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PDBsum entry 1kzg
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Signaling protein
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PDB id
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1kzg
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Contents |
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337 a.a.
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188 a.a.
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177 a.a.
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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A crystallographic view of interactions between dbs and cdc42: ph domain-Assisted guanine nucleotide exchange.
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Authors
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K.L.Rossman,
D.K.Worthylake,
J.T.Snyder,
D.P.Siderovski,
S.L.Campbell,
J.Sondek.
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Ref.
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EMBO J, 2002,
21,
1315-1326.
[DOI no: ]
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PubMed id
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Abstract
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Dbl-related oncoproteins are guanine nucleotide exchange factors (GEFs) specific
for Rho guanosine triphosphatases (GTPases) and invariably possess tandem Dbl
(DH) and pleckstrin homology (PH) domains. While it is known that the DH domain
is the principal catalytic subunit, recent biochemical data indicate that for
some Dbl-family proteins, such as Dbs and Trio, PH domains may cooperate with
their associated DH domains in promoting guanine nucleotide exchange of Rho
GTPases. In order to gain an understanding of the involvement of these PH
domains in guanine nucleotide exchange, we have determined the crystal structure
of a DH/PH fragment from Dbs in complex with Cdc42. The complex features the PH
domain in a unique conformation distinct from the PH domains in the related
structures of Sos1 and Tiam1.Rac1. Consequently, the Dbs PH domain participates
with the DH domain in binding Cdc42, primarily through a set of interactions
involving switch 2 of the GTPase. Comparative sequence analysis suggests that a
subset of Dbl-family proteins will utilize their PH domains similarly to Dbs.
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Figure 4.
Figure 4 Interactions between the PH domain of Dbs and Cdc42.
Stereo view of the PH domain (blue) participating with  6
of the DH domain (yellow) to bind switch 2 (red) and 3b
(green) of Cdc42. Dashed lines indicate hydrogen bonds
(<3.3Å).
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Figure 8.
Figure 8 The structure of Dbs  Cdc42
suggests a model for membrane engagement.
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2002,
21,
1315-1326)
copyright 2002.
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