1t84

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==Overview==
==Overview==
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Current drug discovery efforts focus primarily on proteins with defined, enzymatic or small molecule binding sites. Autoregulatory domains, represent attractive alternative targets for small molecule inhibitors, because they also occur in noncatalytic proteins and because allosteric, inhibitors may avoid specificity problems inherent in active site-directed, inhibitors. We report here the identification of wiskostatin, a chemical, inhibitor of the neural Wiskott-Aldrich syndrome protein (N-WASP)., Wiskostatin interacts with a cleft in the regulatory GTPase-binding domain, (GBD) of WASP in the solution structure of the complex. Wiskostatin, induces folding of the isolated, unstructured GBD into its autoinhibited, conformation, suggesting that wiskostatin functions by stabilizing N-WASP, in its autoinhibited state. The use of small molecules to bias, conformational equilibria represents a potentially general strategy for, chemical inhibition of autoinhibited proteins, even in cases where such, sites have not been naturally evolved in a target.
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Current drug discovery efforts focus primarily on proteins with defined enzymatic or small molecule binding sites. Autoregulatory domains represent attractive alternative targets for small molecule inhibitors because they also occur in noncatalytic proteins and because allosteric inhibitors may avoid specificity problems inherent in active site-directed inhibitors. We report here the identification of wiskostatin, a chemical inhibitor of the neural Wiskott-Aldrich syndrome protein (N-WASP). Wiskostatin interacts with a cleft in the regulatory GTPase-binding domain (GBD) of WASP in the solution structure of the complex. Wiskostatin induces folding of the isolated, unstructured GBD into its autoinhibited conformation, suggesting that wiskostatin functions by stabilizing N-WASP in its autoinhibited state. The use of small molecules to bias conformational equilibria represents a potentially general strategy for chemical inhibition of autoinhibited proteins, even in cases where such sites have not been naturally evolved in a target.
==Disease==
==Disease==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bickford, L.C.]]
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[[Category: Bickford, L C.]]
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[[Category: Kim, A.S.]]
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[[Category: Kim, A S.]]
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[[Category: Kirschner, M.W.]]
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[[Category: Kirschner, M W.]]
[[Category: Morgan, D.]]
[[Category: Morgan, D.]]
[[Category: Ouerfelli, O.]]
[[Category: Ouerfelli, O.]]
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[[Category: Peterson, J.R.]]
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[[Category: Peterson, J R.]]
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[[Category: Rosen, M.K.]]
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[[Category: Rosen, M K.]]
[[Category: WSK]]
[[Category: WSK]]
[[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 16:55:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:53 2008''

Revision as of 13:10, 21 February 2008


1t84

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Solution structure of the Wiskott-Aldrich Syndrome Protein (WASP) autoinhibited core domain complexed with (S)-wiskostatin, a small molecule inhibitor

Contents

Overview

Current drug discovery efforts focus primarily on proteins with defined enzymatic or small molecule binding sites. Autoregulatory domains represent attractive alternative targets for small molecule inhibitors because they also occur in noncatalytic proteins and because allosteric inhibitors may avoid specificity problems inherent in active site-directed inhibitors. We report here the identification of wiskostatin, a chemical inhibitor of the neural Wiskott-Aldrich syndrome protein (N-WASP). Wiskostatin interacts with a cleft in the regulatory GTPase-binding domain (GBD) of WASP in the solution structure of the complex. Wiskostatin induces folding of the isolated, unstructured GBD into its autoinhibited conformation, suggesting that wiskostatin functions by stabilizing N-WASP in its autoinhibited state. The use of small molecules to bias conformational equilibria represents a potentially general strategy for chemical inhibition of autoinhibited proteins, even in cases where such sites have not been naturally evolved in a target.

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

1T84 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Chemical inhibition of N-WASP by stabilization of a native autoinhibited conformation., Peterson JR, Bickford LC, Morgan D, Kim AS, Ouerfelli O, Kirschner MW, Rosen MK, Nat Struct Mol Biol. 2004 Aug;11(8):747-55. Epub 2004 Jul 4. PMID:15235593

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