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1ej5

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==Overview==
==Overview==
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The Rho-family GTPase, Cdc42, can regulate the actin cytoskeleton through, activation of Wiskott-Aldrich syndrome protein (WASP) family members., Activation relieves an autoinhibitory contact between the GTPase-binding, domain and the carboxy-terminal region of WASP proteins. Here we report, the autoinhibited structure of the GTPase-binding domain of WASP, which, can be induced by the C-terminal region or by organic co-solvents. In the, autoinhibited complex, intramolecular interactions with the GTPase-binding, domain occlude residues of the C terminus that regulate the Arp2/3, actin-nucleating complex. Binding of Cdc42 to the GTPase-binding domain, causes a dramatic conformational change, resulting in disruption of the, hydrophobic core and release of the C terminus, enabling its interaction, with the actin regulatory machinery. These data show that 'intrinsically, unstructured' peptides such as the GTPase-binding domain of WASP can be, induced into distinct structural and functional states depending on, context.
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The Rho-family GTPase, Cdc42, can regulate the actin cytoskeleton through activation of Wiskott-Aldrich syndrome protein (WASP) family members. Activation relieves an autoinhibitory contact between the GTPase-binding domain and the carboxy-terminal region of WASP proteins. Here we report the autoinhibited structure of the GTPase-binding domain of WASP, which can be induced by the C-terminal region or by organic co-solvents. In the autoinhibited complex, intramolecular interactions with the GTPase-binding domain occlude residues of the C terminus that regulate the Arp2/3 actin-nucleating complex. Binding of Cdc42 to the GTPase-binding domain causes a dramatic conformational change, resulting in disruption of the hydrophobic core and release of the C terminus, enabling its interaction with the actin regulatory machinery. These data show that 'intrinsically unstructured' peptides such as the GTPase-binding domain of WASP can be induced into distinct structural and functional states depending on context.
==Disease==
==Disease==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Abdul-Manan, N.]]
[[Category: Abdul-Manan, N.]]
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[[Category: Kakalis, L.T.]]
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[[Category: Kakalis, L T.]]
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[[Category: Kim, A.S.]]
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[[Category: Kim, A S.]]
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[[Category: Liu, G.A.]]
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[[Category: Liu, G A.]]
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[[Category: Rosen, M.K.]]
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[[Category: Rosen, M K.]]
[[Category: alpha helix]]
[[Category: alpha helix]]
[[Category: beta-hairpin turn]]
[[Category: beta-hairpin turn]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:43:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:20 2008''

Revision as of 10:28, 21 February 2008


1ej5

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SOLUTION STRUCTURE OF THE AUTOINHIBITED CONFORMATION OF WASP

Contents

Overview

The Rho-family GTPase, Cdc42, can regulate the actin cytoskeleton through activation of Wiskott-Aldrich syndrome protein (WASP) family members. Activation relieves an autoinhibitory contact between the GTPase-binding domain and the carboxy-terminal region of WASP proteins. Here we report the autoinhibited structure of the GTPase-binding domain of WASP, which can be induced by the C-terminal region or by organic co-solvents. In the autoinhibited complex, intramolecular interactions with the GTPase-binding domain occlude residues of the C terminus that regulate the Arp2/3 actin-nucleating complex. Binding of Cdc42 to the GTPase-binding domain causes a dramatic conformational change, resulting in disruption of the hydrophobic core and release of the C terminus, enabling its interaction with the actin regulatory machinery. These data show that 'intrinsically unstructured' peptides such as the GTPase-binding domain of WASP can be induced into distinct structural and functional states depending on context.

Disease

Known diseases associated with this structure: Neutropenia, severe congenital, X-linked OMIM:[300392], Thrombocytopenia, X-linked OMIM:[300392], Thrombocytopenia, X-linked, intermittent OMIM:[300392], Wiskott-Aldrich syndrome OMIM:[300392]

About this Structure

1EJ5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein., Kim AS, Kakalis LT, Abdul-Manan N, Liu GA, Rosen MK, Nature. 2000 Mar 9;404(6774):151-8. PMID:10724160

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