matrixdb Institut de Biologie et de Chimie des Prot\u00c3\u00a9ines, 7, passage du Vercors 69 367 Lyon cedex 07 FRANCE matrixdb@ibcp.fr http://matrixdb.ibcp.fr A single residue, arginine 65, is critical for the functional interaction of leukocyte-associated inhibitory receptor-1 with collagens. A single residue, arginine 65, is critical for the functional interaction of leukocyte-associated inhibitory receptor-1 with collagens. Journal of immunology (Baltimore, Md. : 1950) 2009 imex curation Tang X., Narayanan S., Peruzzi G., Apara A., Natarajan K., Margulies DH., Coligan JE., Borrego F. Francisco.Borrego@fda.hhs.gov 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Tang X., Narayanan S., Peruzzi G., Apara A., Natarajan K., Margulies DH., Coligan JE., Borrego F. Francisco.Borrego@fda.hhs.gov Accepted 2018-SEP-11 AT 08:52 BST AT 08:52 BST by ORCHARD Journal of immunology (Baltimore, Md. : 1950) 2009 Only protein-protein interactions imex curation imex curation Mock publication and experiment for abstract interactions that are not interaction evidences. Mock publication and experiment for abstract interactions that are not interaction evidences. unspecified method lair1_human Leukocyte-associated immunoglobulin-like receptor 1 LAIR1 CD305 protein protein human Homo sapiens Human MSPHPTALLGLVLCLAQTIHTQEEDLPRPSISAEPGTVIPLGSHVTFVCRGPVGVQTFRLERESRSTYNDTEDVSQASPSESEARFRIDSVSEGNAGPYRCIYYKPPKWSEQSDYLELLVKETSGGPDSPDTEPGSSAGPTQRPSDNSHNEHAPASQGLKAEHLYILIGVSVVFLFCLLLLVLFCLHRQNQIKQGPPRSKDEEQKPQQRPDLAVDVLERTADKATVNGLPEKDRETDTSALAAGSSQEVTYAQLDHWALTQRTARAVSPQSTKPMAESITYAAVARH 752EFB2FCC29B8E8 co1a1_rat Collagen alpha-1(I) chain Alpha-1 type I collagen Col1a1 protein protein rat Rattus norvegicus (Rat) Rat MFSFVDLRLLLLLGATALLTHGQEDIPEVSCIHNGLRVPNGETWKPDVCLICICHNGTAVCDGVLCKEDLDCPNPQKREGECCPFCPEEYVSPDAEVIGVEGPKGDPGPQGPRGPVGPPGQDGIPGQPGLPGPPGPPGPPGPPGLGGNFASQMSYGYDEKSAGVSVPGPMGPSGPRGLPGPPGAPGPQGFQGPPGEPGEPGASGPMGPRGPPGPPGKNGDDGEAGKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDTGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGPPGSAGARGNDGAVGAAGPPGPTGPTGPPGFPGAAGAKGEAGPQGARGSEGPQGVRGEPGPPGPAGAAGPAGNPGADGQPGAKGANGAPGIAGAPGFPGARGPSGPQGPSGAPGPKGNSGEPGAPGNKGDTGAKGEPGPAGVQGPPGPAGEEGKRGARGEPGPSGLPGPPGERGGPGSRGFPGADGVAGPKGPAGERGSPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQDGRPGPAGPPGARGQAGVMGFPGPKGTAGEPGKAGERGVPGPPGAVGPAGKDGEAGAQGAPGPAGPAGERGEQGPAGSPGFQGLPGPAGPPGEAGKPGEQGVPGDLGAPGPSGARGERGFPGERGVQGPPGPAGPRGNNGAPGNDGAKGDTGAPGAPGSQGAPGLQGMPGERGAAGLPGPKGDRGDAGPKGADGSPGKDGVRGLTGPIGPPGPAGAPGDKGETGPSGPAGPTGARGAPGDRGEPGPPGPAGFAGPPGADGQPGAKGEPGDTGVKGDAGPPGPAGPAGPPGPIGNVGAPGPKGSRGAAGPPGATGFPGAAGRVGPPGPSGNAGPPGPPGPVGKEGGKGPRGETGPAGRPGEVGPPGPPGPAGEKGSPGADGPAGSPGTPGPQGIAGQRGVVGLPGQRGERGFPGLPGPSGEPGKQGPSGASGERGPPGPMGPPGLAGPPGESGREGSPGAEGSPGRDGAPGAKGDRGETGPAGPPGAPGAPGAPGPVGPAGKNGDRGETGPAGPAGPIGPAGARGPAGPQGPRGDKGETGEQGDRGIKGHRGFSGLQGPPGSPGSPGEQGPSGASGPAGPRGPPGSAGSPGKDGLNGLPGPIGPPGPRGRTGDSGPAGPPGPPGPPGPPGPPSGGYDFSFLPQPPQEKSQDGGRYYRADDANVVRDRDLEVDTTLKSLSQQIENIRSPEGSRKNPARTCRDLKMCHSDWKSGEYWIDPNQGCNLDAIKVYCNMETGQTCVFPTQPSVPQKNWYISPNPKEKKHVWFGESMTDGFQFEYGSEGSDPADVAIQLTFLRLMSTEASQNITYHCKNSVAYMDQQTGNLKKSLLLQGSNEIELRGEGNSRFTYSTLVDGCTSHTGTWGKTVIEYKTTKTSRLPIIDVAPLDIGAPDQEFGMDIGPACFV DIP protein P02454 original sequence version: 131 DIP protein P02454 original sequence version: 142 BCDDC40C3167AE59 co1a2_rat Collagen alpha-2(I) chain Alpha-2 type I collagen Col1a2 protein protein rat Rattus norvegicus (Rat) Rat MLSFVDTRTLLLLAVTSCLATCQSLQMGSVRKGPTGDRGPRGQRGPAGPRGRDGVDGPVGPPGPPGAPGPPGPPGPPGLTGNFAAQYSDKGVSAGPGPMGLMGPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPAGSRGPAGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGELGPVGNPGPAGPAGPRGEAGLPGLSGPVGPPGNPGANGLTGAKGATGLPGVAGAPGLPGPRGIPGPVGAAGATGPRGLVGEPGPAGSKGETGNKGEPGSAGAQGPPGPSGEEGKRGSPGEPGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGSTGPAGVRGPNGDAGRPGEPGLMGPRGLPGSPGNVGPAGKEGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGEKGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTAGEVGKPGERGLPGEFGLPGPAGPRGERGPPGESGAAGPSGPIGIRGPSGAPGPDGNKGEAGAVGAPGSAGASGPGGLPGERGAAGIPGGKGEKGETGLRGEIGNPGRDGARGAPGAIGAPGPAGASGDRGEAGAAGPSGPAGPRGSPGERGEVGPAGPNGFAGPAGSAGQPGAKGEKGTKGPKGENGIVGPTGPVGAAGPSGPNGPPGPAGSRGDGGPPGMTGFPGAAGRTGPPGPSGITGPPGPPGAAGKEGIRGPRGDQGPVGRTGEIGASGPPGFAGEKGPSGEPGTTGPPGTAGPQGLLGAPGILGLPGSRGERGQPGIAGALGEPGPLGIAGPPGARGPPGAVGSPGVNGAPGEAGRDGNPGSDGPPGRDGQPGHKGERGYPGNIGPTGAAGAPGPHGSVGPAGKHGNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGDKGARGLPGLKGHNGLQGLPGLAGLHGDQGAPGPVGPAGPRGPAGPSGPIGKDGRSGHPGPVGPAGVRGSQGSQGPAGPPGPPGPPGPPGVSGGGYDFGFEGGFYRADQPRSQPSLRPKDYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWKSDYYWIDPNQGCTMDAIKVYCDFSTGETCIQAQPVNTPAKNAYSRAQANKHVWLGETINGGSQFEYNAEGVSSKEMATQLAFMRLLANRASQNITYHCKNSIAYLDEETGRLNKAVILQGSNDVELVAEGNSRFTYTVLVDGCSKKTNEWDKTVIEYKTNKPSRLPFLDIAPLDIGGTNQEFRVEVGPVCFK DIP protein P02466 original sequence version: 123 B069371A8DB20A72 collagen_i_rat-lair1-1 1 3 unspecified role unspecified role prey prey Binding site Binding site sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Tag IgG1 tag fc-igg1 fc-igg1 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q6GTX8:p.Arg65Lys Mutation mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain R K Tue Jun 30 18:12:51 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg65Lys' human-293t Homo sapiens 293 cells transformed with SV40 large T antigen 293t 293 cells expressing SV40 large T antigen. The original designation of this cell line was 293tsA1609neo. It is not in Cabri,ATCC or HyperCLDB. 12 unspecified role unspecified role bait bait direct interaction direct interaction Figure 6 A-D collagen_i_rat Type I collagen Collagen type I trimer Type I collagen 2xCOL1A1:COL1A2 4 unspecified role unspecified role co1a2 binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 5 unspecified role unspecified role co1a1 binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 14 16 direct interaction direct interaction rat Rattus norvegicus (Rat) Rat stable complex stable complex physical interaction evidence used in manual assertion physical interaction evidence used in manual assertion IPI inferred from physical interaction Form the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite. Heterotrimer Triple-helices consisting of about 1000 amino acids per chain forming a coiled coil structure. Each polypeptide forms a left-handed helix in which every third residue, glycine, comes into the center of the superhelix. Propeptides (telopeptides) at both ends of the molecular precursor undergo highly complex fibrillogenesis. created with intact-jami-dbscripts