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Structural basis for ubiquitin recognition by the human EAP45/ESCRT-II GLUE domainStructural basis for ubiquitin recognition by the human EAP45/ESCRT-II GLUE domain
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe ESCRT-I and ESCRT-II complexes help sort ubiquitinated proteins into vesicles that accumulate within multivesicular bodies (MVBs). Crystallographic and biochemical analyses reveal that the GLUE domain of the human ESCRT-II EAP45 (also called VPS36) subunit is a split pleckstrin-homology domain that binds ubiquitin along one edge of the beta-sandwich. The structure suggests how human ESCRT-II can couple recognition of ubiquitinated cargoes and endosomal phospholipids during MVB protein sorting. Structural basis for ubiquitin recognition by the human ESCRT-II EAP45 GLUE domain.,Alam SL, Langelier C, Whitby FG, Koirala S, Robinson H, Hill CP, Sundquist WI Nat Struct Mol Biol. 2006 Nov;13(11):1029-30. Epub 2006 Oct 22. PMID:17057716[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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