{"id":"42d1fbea-336f-5506-b9ab-3e5b013c5773","stable_key":"0ad8610d-d575-5870-b7cd-763a9f750783:copper-atox1-atp7b-mobility","predicate":"copper_transfer_increases","statement":"Copper transfer from ATOX1 reduced interactions within ATP7B MBD1-3 and increased domain mobility.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"6e542e0c-5475-57a3-adbc-9356ab082e36","mechanism_event_label":"Copper handoff changes how the pump can move.","subject":{"id":"dfe5c2e7-c502-53b9-9f74-baa41a18c8a9","slug":"atox1","display_name":"Human copper chaperone ATOX1","entity_type_key":"protein"},"object":{"id":"2f95891a-f7c0-504c-9258-ea97d67fb32a","slug":"atp7b-metal-domain-mobility","display_name":"ATP7B N-terminal metal-binding domain mobility","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"6e542e0c-5475-57a3-adbc-9356ab082e36","stable_key":"0ad8610d-d575-5870-b7cd-763a9f750783:copper-atox1-atp7b-mobility-event","event_type":"biochemical_relationship","label":"Copper handoff changes how the pump can move.","description":"Copper transfer from ATOX1 reduced interactions within ATP7B MBD1-3 and increased domain mobility.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"05dae672-bbd9-585d-8713-ccfe9e14d26a","slug":"atp7b","display_name":"Human copper-transporting ATPase ATP7B","entity_type_key":"protein"},"role":"regulated protein","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"dfe5c2e7-c502-53b9-9f74-baa41a18c8a9","slug":"atox1","display_name":"Human copper chaperone ATOX1","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"2f95891a-f7c0-504c-9258-ea97d67fb32a","slug":"atp7b-metal-domain-mobility","display_name":"ATP7B N-terminal metal-binding domain mobility","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/copper-research/28900031.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"64fceb98b5bf2ca406f26799cea5832b0306883118b9ad2416ba87db47b18ce8\", \"start_char\": 0, \"end_char\": 1471, \"text_sha256\": \"64fceb98b5bf2ca406f26799cea5832b0306883118b9ad2416ba87db47b18ce8\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Biochemistry, solution NMR and small-angle X-ray scattering","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Apo versus copper-loaded ATOX1","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Domain motion and ATP hydrolysis were studied directly; these assays do not establish a whole-body copper requirement.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Copper research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"copper","display_name":"Copper","entity_type_key":"nutrient_element"}},{"dimension":"organism","value_text":"Human proteins","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Copper handoff changes how the pump can move.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[copper-p28900031] The metal chaperone Atox1 regulates the activity of the human copper transporter ATP7B by modulating domain dynamics. (2017). https://pubmed.ncbi.nlm.nih.gov/28900031/ DOI: 10.1074/jbc.m117.811752","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified ATOX1 and ATP7B domains","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"fbae6f58-fad9-51dd-b483-b73eb8a71974","evidence_kind":"source_excerpt","locator":"Lines 403-414","start_line":403,"end_line":414,"excerpt":"### copper-atox1-atp7b-mobility\nCopper transfer from ATOX1 reduced interactions within ATP7B MBD1-3 and increased domain mobility.\nCondition category: normal\nnutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Copper handoff changes how the pump can move.\norganism: Human proteins\ntissue_or_cell_type: Purified ATOX1 and ATP7B domains\nexperimental_model: Biochemistry, solution NMR and small-angle X-ray scattering\nlimitations: Domain motion and ATP hydrolysis were studied directly; these assays do not establish a whole-body copper requirement.\nexposure: Apo versus copper-loaded ATOX1\nevidence_span: {\"source_cache\": \"artifacts/copper-research/28900031.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"64fceb98b5bf2ca406f26799cea5832b0306883118b9ad2416ba87db47b18ce8\", \"start_char\": 0, \"end_char\": 1471, \"text_sha256\": \"64fceb98b5bf2ca406f26799cea5832b0306883118b9ad2416ba87db47b18ce8\"}\n[copper-p28900031] The metal chaperone Atox1 regulates the activity of the human copper transporter ATP7B by modulating domain dynamics. 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