2HTH

Structural basis for ubiquitin recognition by the human EAP45/ESCRT-II GLUE domain

Summary for 2HTH

• Entry DOI: 10.2210/pdb2hth/pdb
• Related: 2CAY
• Descriptor: Ubiquitin, Vacuolar protein sorting protein 36 (2 entities in total)
• Functional Keywords: glue domain, ph domain, protein sorting, viral budding, ubiquitin complex, protein transport
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q86VN1
• Total number of polymer chains: 2
• Total formula weight: 24834.48

Authors

Alam, S.L.,Whitby, F.G.,Hill, C.P.,Sundquist, W.I. (deposition date: 2006-07-25, release date: 2006-10-24, Last modification date: 2024-02-14)

Primary citation

Alam, S.L.,Langelier, C.,Whitby, F.G.,Koirala, S.,Robinson, H.,Hill, C.P.,Sundquist, W.I.
Structural basis for ubiquitin recognition by the human ESCRT-II EAP45 GLUE domain.
Nat.Struct.Mol.Biol., 13:1029-1030, 2006

PubMed Abstract: The 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.

PubMed: 17057716
DOI: 10.1038/nsmb1160

Experimental method

X-RAY DIFFRACTION (2.7 Å)