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PDBsum entry 2vrw
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Signaling protein
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PDB id
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2vrw
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References listed in PDB file
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Key reference
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Title
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Crucial structural role for the ph and c1 domains of the vav1 exchange factor.
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Authors
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J.Rapley,
V.L.Tybulewicz,
K.Rittinger.
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Ref.
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Embo Rep, 2008,
9,
655-661.
[DOI no: ]
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PubMed id
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Abstract
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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.
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