{"metadata":{"accession":"PF04380","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR007475","hierarchy":null,"name":{"name":"Membrane fusogenic activity","short":"BMFP"},"description":[{"text":"<p>BMFP consists of two structural domains, a coiled-coil C-terminal domain via which the protein self-associates as a trimer, and an N-terminal domain disordered at neutral pH but adopting an amphipathic alpha-helical structure in the presence of phospholipid vesicles, high ionic strength, acidic pH or SDS. BMFP interacts with phospholipid vesicles though the predicted amphipathic alpha-helix induced in the N-terminal half of the protein and promotes aggregation and fusion of vesicles in vitro.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00079201":{"PMID":18616282,"ISBN":null,"volume":"47","issue":"31","year":2008,"title":"Brucella abortus MFP: a trimeric coiled-coil protein with membrane fusogenic activity.","URL":null,"raw_pages":"8165-75","medline_journal":"Biochemistry","ISO_journal":"Biochemistry","authors":["Carrica Mdel C","Craig PO","Alonso Sdel V","Goldbaum FA","Cravero SL."],"DOI_URL":"http://dx.doi.org/10.1021/bi800462y"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":1,"interactions":0,"matches":6218,"pathways":0,"proteins":6218,"proteomes":6209,"sets":0,"structural_models":{"alphafold":4101},"structures":0,"taxa":8371},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":97,"alignment:full":2901},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}