Switch #:
SWTI000266
Switch type:
Binary
Switch subtype:
Allostery

Description:
Binding of Cell division control protein 42 homolog (CDC42) to Wiskott-Aldrich syndrome protein (WAS) allosterically relieves an auto-inhibitory intramolecular interaction in Wiskott-Aldrich syndrome protein (WAS), which becomes active.

Participants:
(1) Wiskott-Aldrich syndrome protein (WAS)

Interactions
Interaction #1 WAS - WAS(intramolecular)
intramolecular
Interfaces
(1) ELM:LIG_GBD_WASP_1 motif (466LVGALMHVMQK476) in Wiskott-Aldrich syndrome protein (WAS)
(2) P21-Rho-binding domain (237-296) in Wiskott-Aldrich syndrome protein (WAS)

Interaction Regulation
Effector binding Inhibition (Cell division control protein 42 homolog (CDC42)) of the Wiskott-Aldrich syndrome protein (WAS) LIG_GBD_WASP_1 motif - Wiskott-Aldrich syndrome protein (WAS) P21-Rho-binding domain interaction

Additional Information
Structural information: 1EJ5, 1CEE
References

(1) Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein.
Kim et al. Nature (2000)

(2) Physical mechanisms of signal integration by WASP family proteins.
Padrick et al. Annu. Rev. Biochem. (2010)

(3) A two-state allosteric model for autoinhibition rationalizes WASP signal integration and targeting.
Buck et al. J. Mol. Biol. (2004)

(4) The nucleotide switch in Cdc42 modulates coupling between the GTPase-binding and allosteric equilibria of Wiskott-Aldrich syndrome protein.
Leung et al. Proc. Natl. Acad. Sci. U.S.A. (2005)

(5) Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate.
Rohatgi et al. J. Cell Biol. (2000)

(6) Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex.
Prehoda et al. Science (2000)

(7) Structure of Cdc42 in complex with the GTPase-binding domain of the 'Wiskott-Aldrich syndrome' protein.
Abdul-Manan et al. Nature (1999)




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