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 TLR1-TLR2 Heterodimer Induced by Binding of a Tri-Acylated Lipopeptide. Crystal Structure of the TLR1-TLR2 Heterodimer Induced by Binding of a Tri-Acylated Lipopeptide. Cell (0092-8674) 2007 Jin MS., Kim SE., Heo JY., Lee ME., Kim HM., Paik SG., Lee H., Lee JO. Mouse TLR2 was also crystallised with the synthetic bacterial lipoprotein Pam2CSK4 but coordinates do not appear to have been deposited so I have not included this interaction in the entry. davet in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Jin MS., Kim SE., Heo JY., Lee ME., Kim HM., Paik SG., Lee H., Lee JO. Mouse TLR2 was also crystallised with the synthetic bacterial lipoprotein Pam2CSK4 but coordinates do not appear to have been deposited so I have not included this interaction in the entry. Accepted 2007-NOV-31 by DAVET. Cell (0092-8674) 2007 davet tlr1_q4g1l2_protein TV3 Hybrid of human TLR1 and Hagfish VLR protein protein human Homo sapiens Human EFLVDRSKNGLIHVPKDLSQKTTILNISQNYISELWTSDILSLSKLRILIISHNRIQYLDISVFKFNQELEYLDLSHNKLVKISCHPTVNLKHLDLSFNAFDALPICKEFGNMSQLKFLGLSTTHLEKSSVLPIAHLNISKVLLVLGETYGEKEDPEGLQDFNTESLHIVFPTNKEFHFILDVSVKTVANLELSNIKCVLEDNKCSYFLSILAKLQTNPKLSNLTLNNIETTWNSFIRILQLVWHTTVWYFSISNVKLQGQLDFRDFDYSGTSLKALSIHQVVSDVFGFPQSYIYEIFSNMNIKNFTVSGTRMVHMLCPSKISPFLHLDFSNNLLTDTVFENCGHLTELETLILQMNQLKELSKIAEMTTQMKSLQQLDISQNSVSYDEKKGDCSWTKSLLSLNMSSNILTDTIFRCLPPRIKVLDLHSNKIKSIPKQVVKLEALQELNVQLKELALDTNQLKSVPDGIFDRLTSLQKIWLHTNPWDCSCPRIDYLSRWLNKNSQKEQGSAKCSGSGKPVRSIICP An amino acid sequence which is not represented in UniProt 7E586B12F3E55B9C s-[2,3-bis(palmitoyloxy)propyl]-cys-ser-lys-lys-lys-lys S-[ 2,3- bis( palmitoyloxy)-( 2RS)- propyl]-[ R]-cysteinyl-[S]-seryl-[S]-lysyl-[S]-lysyl-[S]-lysyl-[S]-lysine small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) tlr2_q4g1l2_protein TV3 hybrid of human TLR2 and hagfish VLR protein protein human Homo sapiens Human LSCDRNGICKGSSGSLNSIPSGLTEAVKSLDLSNNRITYISNSDLQRCVNLQALVLTSNGINTIEEDSFSSLGSLEHLDLSYNYLSNLSSSWFKPLSSLTFLNLLGNPYKTLGETSLFSHLTKLQILRVGNMDTFTKIQRKDFAGLTFLEELEIDASDLQSYEPKSLKSIQNVSHLILHMKQHILLLEIFVDVTSSVECLELRDTDLDTFHFSELSTGETNSLIKKFTFRNVKITDESLFQVMKLLNQISGLLELEFDDCTLNGVGNFRASDNDRVIDPGKVETLTIRRLHIPRFYLFYDLSTLYSLTERVKRITVENSKVFLVPCLLSQHLKSLEYLDLSENLMVEEYLKNSACEDAWPSLQTLILRQNHLASLEKTGETLLTLKNLTNIDISKNSFHSMPETCQWPEKMKYLNLSSTRIHSVTGCIPKTLEILDVSNNNLNLFSLNLPQLKELYISRNKLMTLPDASLLPMKSVPDGIFDRLTSLQKIWLHTNPWDCSCPRIDYLSRWLNKNSQKEQGSAKCSGSGKPVRSIICPTTTTTTTTTTMPTTTTLPTT An amino acid sequence which is not represented in UniProt Hybrid of Q4G1L2 and O60603 81C848C255C1F2CC tlr1-tlr2-1 1 3 unspecified role unspecified role neutral component neutral component 4 unspecified role unspecified role neutral component neutral component spofr-sf_9 Spodoptera frugiperda insect cells Fall armyworm sf_9 insect cells Derived from pupal ovarian tissue of the fall armyworm Cloned from the parent cell line, IPLB-SF-21-AE (SF-21) derived from immature ovaries of fall armyworm Spodoptera frugiperda pupae cells are susceptible to Baculovirus infection 2 unspecified role unspecified role neutral component neutral component spofr-sf_9 Spodoptera frugiperda insect cells Fall armyworm sf_9 insect cells Derived from pupal ovarian tissue of the fall armyworm Cloned from the parent cell line, IPLB-SF-21-AE (SF-21) derived from immature ovaries of fall armyworm Spodoptera frugiperda pupae cells are susceptible to Baculovirus infection direct interaction direct interaction Fragments of TLR and hagfish VLRB.61 were fused at their conserved LxxLxLxxN sites to aid in crystallisation Here we present the crystal structures of the human TLR1-TLR2-lipopeptide complex 2.10 A 0.244 Two of the three lipid chains of the ligand interact with a pocket in TLR2, and the remaining amide-bound lipid chain is inserted into a narrow channel in TLR1. A TLR1 channel and TLR2 pocket are connected at the dimer interface, forming a long and continuous lipid-binding site. The overall shape of the complex resembles the letter "m" where the two C-terminal domains converge in the middle. The TLR1-fused and TLR2-fused VLR fragments in the complex do not interact with each other or with the TLR fragments since their closest atoms are more than 9 A apart. Fig. 2