3e5h
From Proteopedia
Crystal Structure of Rab28 GTPase in the Active (GppNHp-bound) Form
Structural highlights
DiseaseRAB28_HUMAN Cone rod dystrophy. The disease is caused by mutations affecting the gene represented in this entry.[1] FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedRab GTPases are essential regulators of membrane trafficking. We report crystal structures of Rab28 in the active (GppNHp-bound) and inactive (GDP-3'P-bound) forms at 1.5 and 1.1A resolution. Rab28 is a distant member of the Rab family. While the overall fold of Rab28 resembles that of other Rab GTPases, it undergoes a larger nucleotide-dependent conformational change than other members of this family. Added flexibility resulting from a double-glycine motif at the beginning of switch 2 might partially account for this observation. The double-glycine motif, which is conserved in the Arf family, only occurs in Rab28 and Rab7B of the Rab family, and may have a profound effect on their catalytic activities. Large nucleotide-dependent conformational change in Rab28.,Lee SH, Baek K, Dominguez R FEBS Lett. 2008 Dec 10;582(29):4107-11. Epub 2008 Nov 19. PMID:19026641[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Homo sapiens | Large Structures | Baek K | Dominguez R | Lee SH | Li Y
