1txu
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Crystal Structure of the Vps9 Domain of Rabex-5
OverviewOverview
The Rab5 GTPase, an essential regulator of endocytosis and endosome, biogenesis, is activated by guanine-nucleotide exchange factors (GEFs), that contain a Vps9 domain. Here, we show that the catalytic core of the, Rab GEF Rabex-5 has a tandem architecture consisting of a Vps9 domain, stabilized by an indispensable helical bundle. A family-wide analysis of, Rab specificity demonstrates high selectivity for Rab5 subfamily GTPases., Conserved exchange determinants map to a common surface of the Vps9, domain, which recognizes invariant aromatic residues in the switch regions, of Rab GTPases and selects for the Rab5 subfamily by requiring a small, nonacidic residue preceding a critical phenylalanine in the switch I, region. These and other observations reveal unexpected similarity with the, Arf exchange site in the Sec7 domain.
About this StructureAbout this Structure
1TXU is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structure, exchange determinants, and family-wide rab specificity of the tandem helical bundle and Vps9 domains of Rabex-5., Delprato A, Merithew E, Lambright DG, Cell. 2004 Sep 3;118(5):607-17. PMID:15339665
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