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http://purl.uniprot.org/citations/18539118http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18539118http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18539118http://www.w3.org/2000/01/rdf-schema#comment"ESCRT-II plays a pivotal role in receptor downregulation and multivesicular body biogenesis and is conserved from yeast to humans. The crystal structures of two human ESCRT-II complex structures have been determined at 2.6 and 2.9 A resolution, respectively. The complex has three lobes and contains one copy each of VPS22 and VPS36 and two copies of VPS25. The structure reveals a dynamic helical domain to which both the VPS22 and VPS36 subunits contribute that connects the GLUE domain to the rest of the ESCRT-II core. Hydrodynamic analysis shows that intact ESCRT-II has a compact, closed conformation. ESCRT-II binds to the ESCRT-I VPS28 C-terminal domain subunit through a helix immediately C-terminal to the VPS36-GLUE domain. ESCRT-II is targeted to endosomal membranes by the lipid-binding activities of both the Vps36 GLUE domain and the first helix of Vps22. These data provide a unifying structural and functional framework for the ESCRT-II complex."xsd:string
http://purl.uniprot.org/citations/18539118http://purl.org/dc/terms/identifier"doi:10.1016/j.devcel.2008.04.004"xsd:string
http://purl.uniprot.org/citations/18539118http://purl.org/dc/terms/identifier"doi:10.1016/j.devcel.2008.04.004"xsd:string
http://purl.uniprot.org/citations/18539118http://purl.uniprot.org/core/author"Hurley J.H."xsd:string
http://purl.uniprot.org/citations/18539118http://purl.uniprot.org/core/author"Hurley J.H."xsd:string
http://purl.uniprot.org/citations/18539118http://purl.uniprot.org/core/author"Im Y.J."xsd:string
http://purl.uniprot.org/citations/18539118http://purl.uniprot.org/core/author"Im Y.J."xsd:string
http://purl.uniprot.org/citations/18539118http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18539118http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18539118http://purl.uniprot.org/core/name"Dev. Cell"xsd:string
http://purl.uniprot.org/citations/18539118http://purl.uniprot.org/core/name"Dev. Cell"xsd:string
http://purl.uniprot.org/citations/18539118http://purl.uniprot.org/core/pages"902-913"xsd:string
http://purl.uniprot.org/citations/18539118http://purl.uniprot.org/core/pages"902-913"xsd:string
http://purl.uniprot.org/citations/18539118http://purl.uniprot.org/core/title"Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex."xsd:string
http://purl.uniprot.org/citations/18539118http://purl.uniprot.org/core/title"Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex."xsd:string
http://purl.uniprot.org/citations/18539118http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/18539118http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/18539118http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18539118
http://purl.uniprot.org/citations/18539118http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18539118
http://purl.uniprot.org/citations/18539118http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18539118
http://purl.uniprot.org/citations/18539118http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18539118
http://purl.uniprot.org/uniprot/Q9UK41http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/18539118
http://purl.uniprot.org/uniprot/Q9BRG1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/18539118