IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran. Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran. Cell (0092-8674) 2007 imex curation Kim HM., Park BS., Kim JI., Kim SE., Lee J., Oh SC., Enkhbayar P., Matsushima N., Lee H., Yoo OJ., Lee JO. Native PAGE analysis of TLR4-MD-2 complexes was carried out. The expression system for proteins is found in the pdb entry for the complex. The UniProtKB accession number for the hagfish VLR protein found in the hybrids was determined by taking the appropriate sequence from the pdb entry. (Table S2 was used to help determine this sequence). This sequence was used in MPsrch to find the UniProtKB accession number. The authors specify that the ectodomains of TLR4 and MD-2 form a complex but do not give the ranges of the ectodomains. The UniProtKB entry gives the extracellular domain of TLR4 as aa 26-638. The authors state MD-2 lacks transmembrane and intracellular domains. jieoh.lee@kaist.ac.kr 13-Nov-2007: Contacted by JYOTI. davet Only protein-protein interactions 8 in vitro In vitro crosslink cross-linking study crosslink western blot western blot Immuno blot Immuno blot Kim HM., Park BS., Kim JI., Kim SE., Lee J., Oh SC., Enkhbayar P., Matsushima N., Lee H., Yoo OJ., Lee JO. Native PAGE analysis of TLR4-MD-2 complexes was carried out. The expression system for proteins is found in the pdb entry for the complex. The UniProtKB accession number for the hagfish VLR protein found in the hybrids was determined by taking the appropriate sequence from the pdb entry. (Table S2 was used to help determine this sequence). This sequence was used in MPsrch to find the UniProtKB accession number. The authors specify that the ectodomains of TLR4 and MD-2 form a complex but do not give the ranges of the ectodomains. The UniProtKB entry gives the extracellular domain of TLR4 as aa 26-638. The authors state MD-2 lacks transmembrane and intracellular domains. jieoh.lee@kaist.ac.kr Accepted 2007-NOV-18 by DAVET. 13-Nov-2007: Contacted by JYOTI. Cell (0092-8674) 2007 davet Only protein-protein interactions 8 imex curation Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran. Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran. Cell (0092-8674) 2007 imex curation Kim HM., Park BS., Kim JI., Kim SE., Lee J., Oh SC., Enkhbayar P., Matsushima N., Lee H., Yoo OJ., Lee JO. Native PAGE analysis of TLR4-MD-2 complexes was carried out. The expression system for proteins is found in the pdb entry for the complex. The UniProtKB accession number for the hagfish VLR protein found in the hybrids was determined by taking the appropriate sequence from the pdb entry. (Table S2 was used to help determine this sequence). This sequence was used in MPsrch to find the UniProtKB accession number. The authors specify that the ectodomains of TLR4 and MD-2 form a complex but do not give the ranges of the ectodomains. The UniProtKB entry gives the extracellular domain of TLR4 as aa 26-638. The authors state MD-2 lacks transmembrane and intracellular domains. jieoh.lee@kaist.ac.kr 13-Nov-2007: Contacted by JYOTI. davet Only protein-protein interactions 8 in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Kim HM., Park BS., Kim JI., Kim SE., Lee J., Oh SC., Enkhbayar P., Matsushima N., Lee H., Yoo OJ., Lee JO. Native PAGE analysis of TLR4-MD-2 complexes was carried out. The expression system for proteins is found in the pdb entry for the complex. The UniProtKB accession number for the hagfish VLR protein found in the hybrids was determined by taking the appropriate sequence from the pdb entry. (Table S2 was used to help determine this sequence). This sequence was used in MPsrch to find the UniProtKB accession number. The authors specify that the ectodomains of TLR4 and MD-2 form a complex but do not give the ranges of the ectodomains. The UniProtKB entry gives the extracellular domain of TLR4 as aa 26-638. The authors state MD-2 lacks transmembrane and intracellular domains. jieoh.lee@kaist.ac.kr Accepted 2007-NOV-18 by DAVET. 13-Nov-2007: Contacted by JYOTI. Cell (0092-8674) 2007 davet Only protein-protein interactions 8 imex curation Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran. Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran. Cell (0092-8674) 2007 imex curation Kim HM., Park BS., Kim JI., Kim SE., Lee J., Oh SC., Enkhbayar P., Matsushima N., Lee H., Yoo OJ., Lee JO. Native PAGE analysis of TLR4-MD-2 complexes was carried out. The expression system for proteins is found in the pdb entry for the complex. The UniProtKB accession number for the hagfish VLR protein found in the hybrids was determined by taking the appropriate sequence from the pdb entry. (Table S2 was used to help determine this sequence). This sequence was used in MPsrch to find the UniProtKB accession number. The authors specify that the ectodomains of TLR4 and MD-2 form a complex but do not give the ranges of the ectodomains. The UniProtKB entry gives the extracellular domain of TLR4 as aa 26-638. The authors state MD-2 lacks transmembrane and intracellular domains. jieoh.lee@kaist.ac.kr 13-Nov-2007: Contacted by JYOTI. davet Only protein-protein interactions 8 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Kim HM., Park BS., Kim JI., Kim SE., Lee J., Oh SC., Enkhbayar P., Matsushima N., Lee H., Yoo OJ., Lee JO. Native PAGE analysis of TLR4-MD-2 complexes was carried out. The expression system for proteins is found in the pdb entry for the complex. The UniProtKB accession number for the hagfish VLR protein found in the hybrids was determined by taking the appropriate sequence from the pdb entry. (Table S2 was used to help determine this sequence). This sequence was used in MPsrch to find the UniProtKB accession number. The authors specify that the ectodomains of TLR4 and MD-2 form a complex but do not give the ranges of the ectodomains. The UniProtKB entry gives the extracellular domain of TLR4 as aa 26-638. The authors state MD-2 lacks transmembrane and intracellular domains. jieoh.lee@kaist.ac.kr Accepted 2007-NOV-18 by DAVET. Cell (0092-8674) 2007 davet Only protein-protein interactions 8 imex curation Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran. Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran. Cell (0092-8674) 2007 imex curation Kim HM., Park BS., Kim JI., Kim SE., Lee J., Oh SC., Enkhbayar P., Matsushima N., Lee H., Yoo OJ., Lee JO. Native PAGE analysis of TLR4-MD-2 complexes was carried out. The expression system for proteins is found in the pdb entry for the complex. The UniProtKB accession number for the hagfish VLR protein found in the hybrids was determined by taking the appropriate sequence from the pdb entry. (Table S2 was used to help determine this sequence). This sequence was used in MPsrch to find the UniProtKB accession number. The authors specify that the ectodomains of TLR4 and MD-2 form a complex but do not give the ranges of the ectodomains. The UniProtKB entry gives the extracellular domain of TLR4 as aa 26-638. The authors state MD-2 lacks transmembrane and intracellular domains. jieoh.lee@kaist.ac.kr 13-Nov-2007: Contacted by JYOTI. davet Only protein-protein interactions 8 in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Kim HM., Park BS., Kim JI., Kim SE., Lee J., Oh SC., Enkhbayar P., Matsushima N., Lee H., Yoo OJ., Lee JO. Native PAGE analysis of TLR4-MD-2 complexes was carried out. The expression system for proteins is found in the pdb entry for the complex. The UniProtKB accession number for the hagfish VLR protein found in the hybrids was determined by taking the appropriate sequence from the pdb entry. (Table S2 was used to help determine this sequence). This sequence was used in MPsrch to find the UniProtKB accession number. The authors specify that the ectodomains of TLR4 and MD-2 form a complex but do not give the ranges of the ectodomains. The UniProtKB entry gives the extracellular domain of TLR4 as aa 26-638. The authors state MD-2 lacks transmembrane and intracellular domains. jieoh.lee@kaist.ac.kr Accepted 2007-NOV-18 by DAVET. 13-Nov-2007: Contacted by JYOTI. Cell (0092-8674) 2007 davet Only protein-protein interactions 8 imex curation ly96_mouse Lymphocyte antigen 96 Protein MD-2 ESOP-1 Ly96 Esop1 Md2 protein protein mouse Mus musculus Mouse MLPFILFSTLLSPILTESEKQQWFCNSSDAIISYSYCDHLKFPISISSEPCIRLRGTNGFVHVEFIPRGNLKYLYFNLFISVNSIELPKRKEVLCHGHDDDYSFCRALKGETVNTSIPFSFEGILFPKGHYRCVAEAIAGDTEEKLFCLNFTIIHRRDVN DIP protein Q9JHF9 original sequence version: 80 DIP protein Q9JHF9 original sequence version: 91 E224D17E5D5429E2 tlr4_q4g1l2_protein TV3 Hybrid of human TLR4 and Hagfish VLR protein protein human Homo sapiens Human EPCVEVVPNITYQCMELNFYKIPDNLPFSTKNLDLSFNPLRHLGSYSFFSFPELQVLDLSRCEIQTIEDGAYQSLSHLSTLILTGNPIQSLALGAFSGLSSLQKLVAVETNLASLENFPIGHLKTLKELNVAHNLIQSFKLPEYFSNLTNLEHLDLSSNKIQSIYCTDLRVLHQMPLLNLSLDLSLNPMNFIQPGAFKEIRLKELALDTNQLKSVPDGIFDRLTSLQKIWLHTNPWDCSCPRIDYLSRWLNKNSQKEQGSAKCSGSGKPVRSIICP An amino acid sequence which is not represented in UniProt 87E056E5801AF9D3 tlr4_mouse Toll-like receptor 4 Tlr4 Lps protein protein mouse Mus musculus Mouse MMPPWLLARTLIMALFFSCLTPGSLNPCIEVVPNITYQCMDQKLSKVPDDIPSSTKNIDLSFNPLKILKSYSFSNFSELQWLDLSRCEIETIEDKAWHGLHHLSNLILTGNPIQSFSPGSFSGLTSLENLVAVETKLASLESFPIGQLITLKKLNVAHNFIHSCKLPAYFSNLTNLVHVDLSYNYIQTITVNDLQFLRENPQVNLSLDMSLNPIDFIQDQAFQGIKLHELTLRGNFNSSNIMKTCLQNLAGLHVHRLILGEFKDERNLEIFEPSIMEGLCDVTIDEFRLTYTNDFSDDIVKFHCLANVSAMSLAGVSIKYLEDVPKHFKWQSLSIIRCQLKQFPTLDLPFLKSLTLTMNKGSISFKKVALPSLSYLDLSRNALSFSGCCSYSDLGTNSLRHLDLSFNGAIIMSANFMGLEELQHLDFQHSTLKRVTEFSAFLSLEKLLYLDISYTNTKIDFDGIFLGLTSLNTLKMAGNSFKDNTLSNVFANTTNLTFLDLSKCQLEQISWGVFDTLHRLQLLNMSHNNLLFLDSSHYNQLYSLSTLDCSFNRIETSKGILQHFPKSLAFFNLTNNSVACICEHQKFLQWVKEQKQFLVNVEQMTCATPVEMNTSLVLDFNNSTCYMYKTIISVSVVSVIVVSTVAFLIYHFYFHLILIAGCKKYSRGESIYDAFVIYSSQNEDWVRNELVKNLEEGVPRFHLCLHYRDFIPGVAIAANIIQEGFHKSRKVIVVVSRHFIQSRWCIFEYEIAQTWQFLSSRSGIIFIVLEKVEKSLLRQQVELYRLLSRNTYLEWEDNPLGRHIFWRRLKNALLDGKASNPEQTAEEEQETATWT DIP protein Q9QUK6 original sequence version: 103 DIP protein Q9QUK6 original sequence version: 118 DIP protein Q9QUK6 original sequence version: 71 9C83B59F9A220C17 eritoran tetrasodium Eritoran small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) Eritoran is an analog of lipopolysaccharide (LPS). Eritoran is an analog of lipopolysaccharide (LPS). tlr4_human Toll-like receptor 4 TLR4 hToll protein protein human Homo sapiens Human MMSASRLAGTLIPAMAFLSCVRPESWEPCVEVVPNITYQCMELNFYKIPDNLPFSTKNLDLSFNPLRHLGSYSFFSFPELQVLDLSRCEIQTIEDGAYQSLSHLSTLILTGNPIQSLALGAFSGLSSLQKLVAVETNLASLENFPIGHLKTLKELNVAHNLIQSFKLPEYFSNLTNLEHLDLSSNKIQSIYCTDLRVLHQMPLLNLSLDLSLNPMNFIQPGAFKEIRLHKLTLRNNFDSLNVMKTCIQGLAGLEVHRLVLGEFRNEGNLEKFDKSALEGLCNLTIEEFRLAYLDYYLDDIIDLFNCLTNVSSFSLVSVTIERVKDFSYNFGWQHLELVNCKFGQFPTLKLKSLKRLTFTSNKGGNAFSEVDLPSLEFLDLSRNGLSFKGCCSQSDFGTTSLKYLDLSFNGVITMSSNFLGLEQLEHLDFQHSNLKQMSEFSVFLSLRNLIYLDISHTHTRVAFNGIFNGLSSLEVLKMAGNSFQENFLPDIFTELRNLTFLDLSQCQLEQLSPTAFNSLSSLQVLNMSHNNFFSLDTFPYKCLNSLQVLDYSLNHIMTSKKQELQHFPSSLAFLNLTQNDFACTCEHQSFLQWIKDQRQLLVEVERMECATPSDKQGMPVLSLNITCQMNKTIIGVSVLSVLVVSVVAVLVYKFYFHLMLLAGCIKYGRGENIYDAFVIYSSQDEDWVRNELVKNLEEGVPPFQLCLHYRDFIPGVAIAANIIHEGFHKSRKVIVVVSQHFIQSRWCIFEYEIAQTWQFLSSRAGIIFIVLQKVEKTLLRQQVELYRLLSRNTYLEWEDSVLGRHIFWRRLRKALLDGKSWNPEGTVGTGCNWQEATSI 92C48F55821133E8 tlr4_q4g1l2_tv8_prot TV8 hybrid of human TLR4 and Hagfish VLR protein protein human Homo sapiens Human EPCVEVVPNITYQCMELNFYKIPDNLPFSTKNLDLSFNPLRHLGSYSFFSFPELQVLDLSRCEIQTIEDGAYQSLSHLSTLILTGNPIQSLALGAFSGLSSLQKLVAVETNLASLENFPIGHLKTLKELNVAHNLIQSFKLPEYFSNLTNLEHLDLSSNKIQSIYCTDLRVLHQMPLLNLSLDLSLNPMNFIQPGAFKEIRLHKLTLRNNFDSLNVMKTCIQGLAGLEVHRLVLGEFRNEGNLEKFDKSALEGLCNLTIEEFRLAYLDYYLDDIIDLFNCLTNVSSFSLVSVTIERVKDFSYNFGWQHLELVNCKFGQFPTLKLKSLKRLTFTSNKGGNAFSEVDLPSLEFLDLSRNGLSFKGCCSQSDFGTTSLKYLDLSFNGVITMSSNFLGLEQLEHLDFQHSNLKQMSEFSVFLSLRNLIYLDISHTHTRVAFNGIFNGLSSLEVLKMAGNSFQENFLPDIFTELRNLTFLDLSQCQLEQLSPTAFNSLSSLQVLNMNQLKSVPDGIFDRLTSLQKIWLHTNPWDCSCPRIDYLSRWLNKNSQKEQGSAKCSGSGKPVRSIICPT An amino acid sequence which is not represented in UniProt B45DA18B5B9FD736 ly96_human Lymphocyte antigen 96 Protein MD-2 ESOP-1 LY96 ESOP1 MD2 protein protein human Homo sapiens Human MLPFLFFSTLFSSIFTEAQKQYWVCNSSDASISYTYCDKMQYPISINVNPCIELKRSKGLLHIFYIPRRDLKQLYFNLYITVNTMNLPKRKEVICRGSDDDYSFCRALKGETVNTTISFSFKGIKFSKGKYKCVVEAISGSPEEMLFCLEFVILHQPNSN DIP protein Q9Y6Y9 original sequence version: 79 DIP protein Q9Y6Y9 original sequence version: 86 DIP protein Q9Y6Y9 original sequence version: 109 DIP protein Q9Y6Y9 original sequence version: 112 0F92AFF583637C6B ly96-tlr4 3 7 unspecified role unspecified role neutral component neutral component region ectodomain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm 5 unspecified role unspecified role neutral component neutral component spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm direct interaction direct interaction 1, Table S5 the full-length ectodomains of mouse TLR4 and MD-2 were expressed in cultured insect cells using recombinant baculoviruses. The mouse TLR4 and MD-2 proteins form a stable 1:1 complex and are not separated during purification. In the crystal structure, one molecule of MD-2 binds to each TLR4 2.8 A Rsym or Rmerge = 0.095 (0.31) (Highest resolution shell is shown in parenthesis. A.U. Asymmetric Units) ly96-tlr4_q4g1l2 3 11 unspecified role unspecified role neutral component neutral component spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm 8 unspecified role unspecified role neutral component neutral component 6 unspecified role unspecified role neutral component neutral component spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm direct interaction direct interaction 5, Table S5 Among the hybrids, MD-2-bound TV3 was successfully crystallized with Eritoran and their complex structure was solved 2.8 A Rsym or Rmerge = 0.089 (0.38) (Highest resolution shell is shown in parenthesis. A.U. Asymmetric Units) ly96-tlr4_q4g1l2_tv8 2 11 unspecified role unspecified role neutral component neutral component trini-high_5 Trichoplusia ni cell line from eggs high_5 Insect cell line from Trichoplusia ni egg cells Invitrogen supplies this cell line. Invitrogen supply this cell line. 10 unspecified role unspecified role neutral component neutral component trini-high_5 Trichoplusia ni cell line from eggs high_5 Insect cell line from Trichoplusia ni egg cells Invitrogen supplies this cell line. Invitrogen supply this cell line. physical association physical association 6 A Lipolysaccharide (LPS) - The hMD-2-TV8 complex dimerizes in thepresence of LPS. MW = 150 kDa The hMD-2-TV8 complex does not dimerize in the presence of the LPS analog Eritoran. The central and/or C-terminal domains of TLR4 are required for the receptor dimerization because the TV3 hybrid that contains only the N-terminal domain and a part of the central domain interacts normally with MD-2 but did not form a heterotetramer after LPS binding ly96-tlr4-1 2 7 unspecified role unspecified role neutral component neutral component trini-high_5 Trichoplusia ni cell line from eggs high_5 Insect cell line from Trichoplusia ni egg cells Invitrogen supplies this cell line. Invitrogen supply this cell line. 5 unspecified role unspecified role neutral component neutral component trini-high_5 Trichoplusia ni cell line from eggs high_5 Insect cell line from Trichoplusia ni egg cells Invitrogen supplies this cell line. Invitrogen supply this cell line. physical association physical association 6 A LPS bound TLR4-MD-2 eluted earlier in gel filtration chromatography and shifted upwards in native gel electrophoresis. The elution volume of the LPS-bound protein complex in the gel filtration chromatography was consistent with the predicted elution volume of a TLR4-MD-2 heterotetramer Lipopolysaccharide (LPS) - The mMD-2-mTLR4 complex dimerizes in the presence of LPS. MW = 160 kDa The mMD-2-mTLR4 complex does not dimerize in the presence of the LPS analog Eritoran. ly96-tlr4-2 2 9 unspecified role unspecified role neutral component neutral component trini-high_5 Trichoplusia ni cell line from eggs high_5 Insect cell line from Trichoplusia ni egg cells Invitrogen supplies this cell line. Invitrogen supply this cell line. 11 unspecified role unspecified role neutral component neutral component trini-high_5 Trichoplusia ni cell line from eggs high_5 Insect cell line from Trichoplusia ni egg cells Invitrogen supplies this cell line. Invitrogen supply this cell line. physical association physical association 6 A LPS bound TLR4-MD-2 eluted earlier in gel filtration chromatography and shifted upwards in native gel electrophoresis. The elution volume of the LPS-bound protein complex in the gel filtration chromatography was consistent with the predicted elution volume of a TLR4-MD-2 heterotetramer MW = 160 kDa Lipopolysaccharide (LPS) - The hMD-2-hTLR4 complex dimerizes in the presence of LPS. The hMD-2-hTLR4 complex does not dimerize in the presence of the LPS analog Eritoran. ly96-tlr4-3 4 9 unspecified role unspecified role neutral component neutral component trini-high_5 Trichoplusia ni cell line from eggs high_5 Insect cell line from Trichoplusia ni egg cells Invitrogen supplies this cell line. Invitrogen supply this cell line. 10 unspecified role unspecified role neutral component neutral component trini-high_5 Trichoplusia ni cell line from eggs high_5 Insect cell line from Trichoplusia ni egg cells Invitrogen supplies this cell line. Invitrogen supply this cell line. physical association physical association 6 B The central and/or C-terminal domains of TLR4 are required for the receptor dimerization because the TV3 hybrid that contains only the N-terminal domain and a part of the central domain interacts normally with MD-2 but did not form a heterotetramer after LPS binding. Lipopolysaccharide (LPS) - The hMD-2-TV8 complex dimerizes in the presence of LPS. The hMD-2-TV8 complex does not dimerize in the presence of the LPS analog Eritoran. ly96-tlr4-4 4 11 unspecified role unspecified role neutral component neutral component Q9Y6Y9:p.His155Ala mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain H A Wed May 02 17:52:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'his155ala' Tue Jun 30 18:11:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.His155Ala' Q9Y6Y9:p.Phe126Ala mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain F A Wed May 02 18:02:34 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe126ala' Tue Jun 30 18:02:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe126Ala' trini-high_5 Trichoplusia ni cell line from eggs high_5 Insect cell line from Trichoplusia ni egg cells Invitrogen supplies this cell line. Invitrogen supply this cell line. 9 unspecified role unspecified role neutral component neutral component trini-high_5 Trichoplusia ni cell line from eggs high_5 Insect cell line from Trichoplusia ni egg cells Invitrogen supplies this cell line. Invitrogen supply this cell line. physical association physical association 6 B Lipopolysaccharide (LPS) - The hMD-2-hTLR4 complex dimerizes in the presence of LPS. The hMD-2-hTLR4 complex does not dimerize in the presence of the LPS analog Eritoran. Phe126 and His155 mutants of MD-2 bound as normal to TLR4 and LPS, but their complex with TLR4 was not dimerized by LPS. Val82 and Met85 are located close to Phe126 and His155 but altering them by mutation did not affect multimerization. This confirms that the Phe126 and His155 residues play specific roles in receptor dimerization. ly96-tlr4-5 4 7 unspecified role unspecified role neutral component neutral component trini-high_5 Trichoplusia ni cell line from eggs high_5 Insect cell line from Trichoplusia ni egg cells Invitrogen supplies this cell line. Invitrogen supply this cell line. 5 unspecified role unspecified role neutral component neutral component trini-high_5 Trichoplusia ni cell line from eggs high_5 Insect cell line from Trichoplusia ni egg cells Invitrogen supplies this cell line. Invitrogen supply this cell line. physical association physical association 6 B Lipolysaccharide (LPS) - The mMD-2-mTLR4 complex dimerizes in the presence of LPS. The mMD-2-mTLR4 complex does not dimerize in the presence of the LPS analog Eritoran. ly96-tlr4-6 1 9 unspecified role unspecified role neutral component neutral component region ectodomain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain trini-high_5 Trichoplusia ni cell line from eggs high_5 Insect cell line from Trichoplusia ni egg cells Invitrogen supplies this cell line. Invitrogen supply this cell line. 11 unspecified role unspecified role neutral component neutral component trini-high_5 Trichoplusia ni cell line from eggs high_5 Insect cell line from Trichoplusia ni egg cells Invitrogen supplies this cell line. Invitrogen supply this cell line. physical association physical association 6 C the LPS-bound TLR4- MD-2 formed a band consistent with the size of the TLR4-MD-2 heterotetramer after crosslinking with glutaraldehyde and SDS gel electrophoresis Lipolysaccharide (LPS) - The hMD-2-hTLR4 complex dimerizes in the presence of LPS. MW = 175 kDa