{"id":"3a8ae49f-031c-5c41-8f68-50eb91e0639b","stable_key":"4fef8d72-f107-5eb5-b2fb-483ca85465e0:k2-ggcx-osteocalcin-binding","predicate":"precursor_binding_organizes","statement":"Vitamin K-dependent protein propeptide binding stabilized GGCX transmembrane helices 6 and 7 and created its vitamin-K-binding pocket.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"bb258309-61aa-53a4-855d-4c6bfcc5b6ce","mechanism_event_label":"The target protein helps organize the enzyme that modifies it.","subject":{"id":"b043ce5c-8537-5099-8421-b07ec993dbde","slug":"bglap","display_name":"Osteocalcin / BGLAP","entity_type_key":"protein"},"object":{"id":"8889bae4-1223-5f80-b651-0c42190322a9","slug":"ggcx","display_name":"Gamma-glutamyl carboxylase / GGCX","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"bb258309-61aa-53a4-855d-4c6bfcc5b6ce","stable_key":"4fef8d72-f107-5eb5-b2fb-483ca85465e0:k2-ggcx-osteocalcin-binding-event","event_type":"biochemical_relationship","label":"The target protein helps organize the enzyme that modifies it.","description":"Vitamin K-dependent protein propeptide binding stabilized GGCX transmembrane helices 6 and 7 and created its vitamin-K-binding pocket.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"b043ce5c-8537-5099-8421-b07ec993dbde","slug":"bglap","display_name":"Osteocalcin / BGLAP","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"8889bae4-1223-5f80-b651-0c42190322a9","slug":"ggcx","display_name":"Gamma-glutamyl carboxylase / GGCX","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/k2-research/39880952.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"eb8e6d00eecd7c5c780921cae3f804fab60e919301eeb16e9909f36293aaa653\", \"start_char\": 0, \"end_char\": 1230, \"text_sha256\": \"eb8e6d00eecd7c5c780921cae3f804fab60e919301eeb16e9909f36293aaa653\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Cryo-EM, binding, cell assays and molecular dynamics","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Apo, osteocalcin-bound and vitamin-K-bound structures","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Shared vitamin K chemistry; the abstract does not establish K2 exclusivity or identical kinetics for every menaquinone.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"k2","display_name":"Vitamin K2 / menaquinone family","entity_type_key":"chemical_species"}},{"dimension":"organism","value_text":"Human GGCX","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"The target protein helps organize the enzyme that modifies it.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[k2-p39880952] Structure and mechanism of vitamin-K-dependent γ-glutamyl carboxylase. (2025). https://pubmed.ncbi.nlm.nih.gov/39880952/ DOI: 10.1038/s41586-024-08484-9","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Endoplasmic-reticulum membrane enzyme","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"3a3ea707-9ac9-5f82-846e-469faf193d63","evidence_kind":"source_excerpt","locator":"Lines 383-394","start_line":383,"end_line":394,"excerpt":"### k2-ggcx-osteocalcin-binding\nVitamin K-dependent protein propeptide binding stabilized GGCX transmembrane helices 6 and 7 and created its vitamin-K-binding pocket.\nCondition category: normal\nnutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The target protein helps organize the enzyme that modifies it.\norganism: Human GGCX\ntissue_or_cell_type: Endoplasmic-reticulum membrane enzyme\nexperimental_model: Cryo-EM, binding, cell assays and molecular dynamics\nlimitations: Shared vitamin K chemistry; the abstract does not establish K2 exclusivity or identical kinetics for every menaquinone.\nexposure: Apo, osteocalcin-bound and vitamin-K-bound structures\nevidence_span: {\"source_cache\": \"artifacts/k2-research/39880952.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"eb8e6d00eecd7c5c780921cae3f804fab60e919301eeb16e9909f36293aaa653\", \"start_char\": 0, \"end_char\": 1230, \"text_sha256\": \"eb8e6d00eecd7c5c780921cae3f804fab60e919301eeb16e9909f36293aaa653\"}\n[k2-p39880952] Structure and mechanism of vitamin-K-dependent γ-glutamyl carboxylase. 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