First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.
|2vrw, resolution 1.85Å ()|
|Related:||1e96, 1i4d, 1foe, 1mh1, 1i4l, 1he1, 1ryf, 1k1z, 1ryh, 1hh4, 1gcp, 1g4u, 2fju, 1f5x, 1i4t, 1gcq|
CRITICAL STRUCTURAL ROLE FOR THE PH AND C1 DOMAINS OF THE VAV1 EXCHANGE FACTOR
The Vav family of proteins are guanine nucleotide exchange factors (GEFs) for the Rho family of GTPases, which regulate various cellular functions, including T-cell activation. They contain a catalytic Dbl homology (DH) domain that is invariably followed by a pleckstrin homology (PH) domain, which is often required for catalytic activity. Vav proteins are the first GEFs for which an additional C1 domain is required for full biological activity. Here, we present the structure of a Vav1 fragment comprising the DH-PH-C1 domains bound to Rac1. This structure shows that the PH and C1 domains form a single structural unit that packs against the carboxy-terminal helix of the DH domain to stabilize its conformation and to promote nucleotide exchange. In contrast to previous reports, this structure shows that there are no direct contacts between the GTPase and C1 domain but instead suggests new mechanisms for the regulation of Vav1 activity.
Crucial structural role for the PH and C1 domains of the Vav1 exchange factor., Rapley J, Tybulewicz VL, Rittinger K, EMBO Rep. 2008 Jul;9(7):655-61. Epub 2008 May 30. PMID:18511940
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.