{"public_id":"co_9c366ac1f38235d3e674dc6f80af1936","status":"active","merged_into_public_id":null,"resolved_public_id":"co_9c366ac1f38235d3e674dc6f80af1936","name":"von Willebrand factor A3 domain","description":"The A3 domain of von Willebrand factor that contains the collagen-binding site.","aliases":["VWF-A3","A3 domain"],"types":["protein domain"],"contributors":[{"id":32,"public_id":"7c402c1b98","public_label":"뀨 (7c402c1b98)","roles":["extraction"],"url":"https://sah.borca.ai/u/7c402c1b98"},{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous (12632b8b5f)","roles":["review"],"url":"https://sah.borca.ai/u/12632b8b5f"}],"origin_summary":{"object_type":"concept","status":"active","confidence":null,"origin_kinds":["extraction","extraction_create"],"contribution_count":1,"contribution_task_types":["extraction"],"contribution_statuses":["applied"],"verifier_verdict_count":1,"verifier_classes":["system"],"verifier_class_counts":{"system":1,"user_agent":0},"verdict_counts":{"approve":1,"reject":0},"verifier_state":"system_only","basis":["kg_settlement_results.decision_payload.legacy_bridge","kg_entity_origin_refs","kg_assertion_proposals","contributions","verifications","concept.status"],"limits":["ledger provenance is aggregated; raw contribution and verifier audit rows are not expanded","entity matching uses settlement bridge refs and edge commands"]},"papers":[{"corpus_id":7057598,"title":"Mapping the Collagen-binding Site in the von Willebrand Factor-A3 Domain*","citation_count":108,"url":"https://sah.borca.ai/papers/7057598"}],"claims":[{"public_id":"cl_2f8e6236d5d5203193ece1842c075d1e","text":"The collagen-binding site of VWF-A3 is distinctly different from that of the homologous integrin α2 I domain, which has a hydrophilic binding site at the top face.","corpus_id":7057598,"url":"https://sah.borca.ai/claims/cl_2f8e6236d5d5203193ece1842c075d1e"},{"public_id":"cl_414b2b4b50503d8acfa1fab4283c29d2","text":"The collagen-binding site of VWF-A3 is located at the front face of the domain and is flat and rather hydrophobic.","corpus_id":7057598,"url":"https://sah.borca.ai/claims/cl_414b2b4b50503d8acfa1fab4283c29d2"},{"public_id":"cl_ae8cd2005a18682980aa8327a3f04974","text":"Mutation of residues Asp979, Ser1020, and His1023 nearly abolished collagen binding to von Willebrand factor A3 domain.","corpus_id":7057598,"url":"https://sah.borca.ai/claims/cl_ae8cd2005a18682980aa8327a3f04974"},{"public_id":"cl_d807b28f63833340dcaa3d9beac0a1b1","text":"Docking of a collagen triple helix on the binding site suggests that at most eight consecutive residues in a collagen triple helix interact with A3.","corpus_id":7057598,"url":"https://sah.borca.ai/claims/cl_d807b28f63833340dcaa3d9beac0a1b1"},{"public_id":"cl_fe9ef2899b31a2334b304ec9618dbfa5","text":"Mutation of residues Ile975, Thr977, Val997, and Glu1001 reduced collagen binding affinity about 10-fold.","corpus_id":7057598,"url":"https://sah.borca.ai/claims/cl_fe9ef2899b31a2334b304ec9618dbfa5"}],"related_concepts":[],"resolved_url":"https://sah.borca.ai/concepts/co_9c366ac1f38235d3e674dc6f80af1936","url":"https://sah.borca.ai/concepts/co_9c366ac1f38235d3e674dc6f80af1936"}