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/ Molecular and structural basis of cytokine receptor pleiotropy in the interleukin-4/13 system. Molecular and structural basis of cytokine receptor pleiotropy in the interleukin-4/13 system. Cell (0092-8674) 2008 imex curation LaPorte SL., Juo ZS., Vaclavikova J., Colf LA., Qi X., Heller NM., Keegan AD., Garcia KC. The ranges of the proteins and cell type used for expression of proteins were found in the pdb file for crystal structure of the complexes. kcgarcia@stanford.edu 14-May-2008: Contacted by JYOTI. orchard Only protein-protein interactions 10 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. molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined LaPorte SL., Juo ZS., Vaclavikova J., Colf LA., Qi X., Heller NM., Keegan AD., Garcia KC. The ranges of the proteins and cell type used for expression of proteins were found in the pdb file for crystal structure of the complexes. kcgarcia@stanford.edu Accepted 2008-MAY-28 by ORCHARD. 14-May-2008: Contacted by JYOTI. Cell (0092-8674) 2008 orchard Only protein-protein interactions 10 imex curation Molecular and structural basis of cytokine receptor pleiotropy in the interleukin-4/13 system. Molecular and structural basis of cytokine receptor pleiotropy in the interleukin-4/13 system. Cell (0092-8674) 2008 imex curation LaPorte SL., Juo ZS., Vaclavikova J., Colf LA., Qi X., Heller NM., Keegan AD., Garcia KC. The ranges of the proteins and cell type used for expression of proteins were found in the pdb file for crystal structure of the complexes. kcgarcia@stanford.edu 14-May-2008: Contacted by JYOTI. orchard Only protein-protein interactions 10 in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined LaPorte SL., Juo ZS., Vaclavikova J., Colf LA., Qi X., Heller NM., Keegan AD., Garcia KC. The ranges of the proteins and cell type used for expression of proteins were found in the pdb file for crystal structure of the complexes. kcgarcia@stanford.edu Accepted 2008-MAY-28 by ORCHARD. 14-May-2008: Contacted by JYOTI. Cell (0092-8674) 2008 orchard Only protein-protein interactions 10 imex curation Molecular and structural basis of cytokine receptor pleiotropy in the interleukin-4/13 system. Molecular and structural basis of cytokine receptor pleiotropy in the interleukin-4/13 system. Cell (0092-8674) 2008 imex curation LaPorte SL., Juo ZS., Vaclavikova J., Colf LA., Qi X., Heller NM., Keegan AD., Garcia KC. The ranges of the proteins and cell type used for expression of proteins were found in the pdb file for crystal structure of the complexes. kcgarcia@stanford.edu 14-May-2008: Contacted by JYOTI. orchard Only protein-protein interactions 10 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined LaPorte SL., Juo ZS., Vaclavikova J., Colf LA., Qi X., Heller NM., Keegan AD., Garcia KC. The ranges of the proteins and cell type used for expression of proteins were found in the pdb file for crystal structure of the complexes. kcgarcia@stanford.edu Accepted 2008-MAY-28 by ORCHARD. 14-May-2008: Contacted by JYOTI. Cell (0092-8674) 2008 orchard Only protein-protein interactions 10 imex curation il4ra_human Interleukin-4 receptor subunit alpha IL4R 582J2.1 IL4RA protein protein human Homo sapiens Human MGWLCSGLLFPVSCLVLLQVASSGNMKVLQEPTCVSDYMSISTCEWKMNGPTNCSTELRLLYQLVFLLSEAHTCIPENNGGAGCVCHLLMDDVVSADNYTLDLWAGQQLLWKGSFKPSEHVKPRAPGNLTVHTNVSDTLLLTWSNPYPPDNYLYNHLTYAVNIWSENDPADFRIYNVTYLEPSLRIAASTLKSGISYRARVRAWAQCYNTTWSEWSPSTKWHNSYREPFEQHLLLGVSVSCIVILAVCLLCYVSITKIKKEWWDQIPNPARSRLVAIIIQDAQGSQWEKRSRGQEPAKCPHWKNCLTKLLPCFLEHNMKRDEDPHKAAKEMPFQGSGKSAWCPVEISKTVLWPESISVVRCVELFEAPVECEEEEEVEEEKGSFCASPESSRDDFQEGREGIVARLTESLFLDLLGEENGGFCQQDMGESCLLPPSGSTSAHMPWDEFPSAGPKEAPPWGKEQPLHLEPSPPASPTQSPDNLTCTETPLVIAGNPAYRSFSNSLSQSPCPRELGPDPLLARHLEEVEPEMPCVPQLSEPTTVPQPEPETWEQILRRNVLQHGAAAAPVSAPTSGYQEFVHAVEQGGTQASAVVGLGPPGEAGYKAFSSLLASSAVSPEKCGFGASSGEEGYKPFQDLIPGCPGDPAPVPVPLFTFGLDREPPRSPQSSHLPSSSPEHLGLEPGEKVEDMPKPPLPQEQATDPLVDSLGSGIVYSALTCHLCGHLKQCHGQEDGGQTPVMASPCCGCCCGDRSSPPTTPLRAPDPSPGGVPLEASLCPASLAPSGISEKSKSSSSFHPAPGNAQSSSQTPKIVNFVSVGPTYMRVS 9F886DF5612297F8 i13r1_human Interleukin-13 receptor subunit alpha-1 Cancer/testis antigen 19 IL13RA1 IL13R IL13RA protein protein human Homo sapiens Human MEWPARLCGLWALLLCAGGGGGGGGAAPTETQPPVTNLSVSVENLCTVIWTWNPPEGASSNCSLWYFSHFGDKQDKKIAPETRRSIEVPLNERICLQVGSQCSTNESEKPSILVEKCISPPEGDPESAVTELQCIWHNLSYMKCSWLPGRNTSPDTNYTLYYWHRSLEKIHQCENIFREGQYFGCSFDLTKVKDSSFEQHSVQIMVKDNAGKIKPSFNIVPLTSRVKPDPPHIKNLSFHNDDLYVQWENPQNFISRCLFYEVEVNNSQTETHNVFYVQEAKCENPEFERNVENTSCFMVPGVLPDTLNTVRIRVKTNKLCYEDDKLWSNWSQEMSIGKKRNSTLYITMLLIVPVIVAGAIIVLLLYLKRLKIIIFPPIPDPGKIFKEMFGDQNDDTLHWKKYDIYEKQTKEETDSVVLIENLKKASQ DIP protein P78552 original sequence version: 96 5983B3E8F554107B il13_human Interleukin-13 IL13 NC30 protein protein human Homo sapiens Human MHPLLNPLLLALGLMALLLTTVIALTCLGGFASPGPVPPSTALRELIEELVNITQNQKAPLCNGSMVWSINLTAGMYCAALESLINVSGCSAIEKTQRMLSGFCPHKVSAGQFSSLHVRDTKIEVAQFVKDLLLHLKKLFREGRFN DIP protein P35225 original sequence version: 112 BE2D46CCF913D129 il2rg_human Cytokine receptor common subunit gamma IL2RG p64 gammaC Interleukin-2 receptor subunit gamma protein protein human Homo sapiens Human MLKPSLPFTSLLFLQLPLLGVGLNTTILTPNGNEDTTADFFLTTMPTDSLSVSTLPLPEVQCFVFNVEYMNCTWNSSSEPQPTNLTLHYWYKNSDNDKVQKCSHYLFSEEITSGCQLQKKEIHLYQTFVVQLQDPREPRRQATQMLKLQNLVIPWAPENLTLHKLSESQLELNWNNRFLNHCLEHLVQYRTDWDHSWTEQSVDYRHKFSLPSVDGQKRYTFRVRSRFNPLCGSAQHWSEWSHPIHWGSNTSKENPFLFALEAVVISVGSMGLIISLLCVYFWLERTMPRIPTLKNLEDLVTEYHGNFSAWSGVSKGLAESLQPDYSERLCLVSEIPPKGGALGEGPGASPCNQHSPYWAPPCYTLKPET 3B6215246D610215 il4_human Interleukin-4 IL4 B-cell stimulatory factor 1 Lymphocyte stimulatory factor 1 Binetrakin Pitrakinra protein protein human Homo sapiens Human MGLTSQLLPPLFFLLACAGNFVHGHKCDITLQEIIKTLNSLTEQKTLCTELTVTDIFAASKNTTEKETFCRAATVLRQFYSHHEKDTRCLGATAQQFHRHKQLIRFLKRLDRNLWGLAGLNSCPVKEANQSTLENFLERLKTIMREKYSKCSS 8725BF64B34D45F7 il4-il4r 3 7 unspecified role unspecified role neutral component neutral component region 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 8 unspecified role unspecified role neutral component neutral component c-terminal 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 4 unspecified role unspecified role neutral component neutral component region 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 direct interaction direct interaction S1 and S2, Table S1 2.95 A R free = 29.7; R cryst = 22.6 Here we present the crystal structures of the complete set of type I (IL-4Ra/gc/IL-4) and type II (IL-4Ra/IL-13Ra1/IL-4, IL-4Ra/IL-13Ra1/IL-13) ternary signaling complexes. il4-il4r-2 3 5 unspecified role unspecified role neutral component neutral component region 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 4 unspecified role unspecified role neutral component neutral component region 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 8 unspecified role unspecified role neutral component neutral component c-terminal 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 direct interaction direct interaction Here we present the crystal structures of the complete set of type I (IL-4Ra/gc/IL-4) and type II (IL-4Ra/IL-13Ra1/ IL-4, IL-4Ra/IL-13Ra1/IL-13) ternary signaling complexes. S1, S2, Table S1 3.0 A R free = 30.4; R cryst = 23.8 il13-il13ra1 3 5 unspecified role unspecified role neutral component neutral component region 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 4 unspecified role unspecified role neutral component neutral component region 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 6 unspecified role unspecified role neutral component neutral component direct interaction direct interaction S1, S2, Table S1 Here we present the crystal structures of the complete set of type I (IL-4Ra/gc/IL-4) and type II (IL-4Ra/IL-13Ra1/IL-4, IL-4Ra/IL-13Ra1/IL-13) ternary signaling complexes. il13-il13ra1-1 1 5 unspecified role unspecified role neutral component neutral component region Ectodomain D1 required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role neutral component neutral component physical association physical association S5 A, B Full length IL-13R ectodomain forms binary complex with IL-13 on gel filtration. The IL-13Ralpha1 D1 domain is required for IL-13 binding. il4-il13ra1-2 1 5 unspecified role unspecified role neutral component neutral component region Ectodomain D2D3 required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain 8 unspecified role unspecified role neutral component neutral component physical association physical association S5 C Truncated IL-13R1 D2D3 ectodomain forms ternary complex with IL-4 on gel filtration. The IL-13Ralpha1 D1 domain is required for IL-13 binding but not IL-4 binding. il4-il4r-3 2 8 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. 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. 4 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. direct interaction direct interaction 3 A, Table S3 we find in the type I complex that IL-4 first binds to IL-4Ra, followed by recruitment of gc to form a ternary complex IL-4 first binds to IL-4Ra, followed by recruitment of gammac to form a ternary complex. The Kd of IL-4 binding to IL-4Ralpha = 1.0 E-9 M; the Kd of gammac binding to IL-4/IL-4Ralpha = 5.59 E-7 M. il4-il4r-4 2 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. 8 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. 4 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. direct interaction direct interaction 3 B, Table S3 For the type II IL-4 complex, IL-4 again first binds to IL-4Ra followed by recruitment of IL-13Ra1 For the type II IL-4 complex, IL-4 first binds to IL-4Ra followed by recruitment of IL-13Ralpha1. Kd for binding of IL-4 to IL-4Ralpha = 1.0 E-9 M; Kd of binding of IL-13Ralpha1 to IL-4/IL-4Ralpha = 4.87 E-7 M il13-il13ra1-2 2 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. 6 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. 4 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. direct interaction direct interaction 3 C, Table S3 for the type II IL-13 complex, IL-13 first binds IL-13Ra1 with an affinity of Kd = 30 nM(similar to previous BIAcore studies [Kd = 34 nM]; Andrews et al., 2002) and this binary complex then recruits IL-4Ra For the IL-13 complex, IL-13 first binds IL-13Ralpha1 and this binary complex then recruits IL-4Ralpha. Kd for IL-13 binding to IL-13Ralpha1 = 3.0 E-8 M; Kd for binding of IL-4Ralpha to IL-13/IL-13Ralpha1 = 2.0 E-8 il4-il4r-5 2 4 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. 8 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. direct interaction direct interaction 3 A, B, Table S3 For the type II IL-4 complex, IL-4 again first binds to IL-4Ra followed by recruitment of IL-13Ra1 Kd for binding of IL-4 to IL-4Ralpha = 1.0 E-9 M il13-il13ra1-3 2 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. 6 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. direct interaction direct interaction 3 C, Table S3 for the type II IL-13 complex, IL-13 first binds IL-13Ra1 with an affinity of Kd = 30 nM(similar to previous BIAcore studies [Kd = 34 nM]; Andrews et al., 2002) and this binary complex then recruits IL-4Ra Kd for IL-13 binding to IL-13Ralpha1 = 3.0 E-8 M