1EJ5
SOLUTION STRUCTURE OF THE AUTOINHIBITED CONFORMATION OF WASP
Summary for 1EJ5
| Entry DOI | 10.2210/pdb1ej5/pdb |
| Related | 1CEE |
| Descriptor | WISKOTT-ALDRICH SYNDROME PROTEIN (1 entity in total) |
| Functional Keywords | alpha helix, beta-hairpin turn, blood clotting |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 11603.60 |
| Authors | Kim, A.S.,Kakalis, L.T.,Abdul-Manan, N.,Liu, G.A.,Rosen, M.K. (deposition date: 2000-02-29, release date: 2000-04-05, Last modification date: 2024-05-22) |
| Primary citation | Kim, A.S.,Kakalis, L.T.,Abdul-Manan, N.,Liu, G.A.,Rosen, M.K. Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature, 404:151-158, 2000 Cited by PubMed Abstract: 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. PubMed: 10724160DOI: 10.1038/35010088 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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