1MKE
Structure of the N-WASP EVH1 Domain-WIP complex
Summary for 1MKE
| Entry DOI | 10.2210/pdb1mke/pdb |
| NMR Information | BMRB: 5554 |
| Descriptor | Fusion protein consisting of Wiskott-Aldrich syndrome protein interacting protein (WIP), GSGSG linker, and Neural Wiskott-Aldrich syndrome protein (N-WASP) (1 entity in total) |
| Functional Keywords | polyproline, protein-protein complex, protein binding |
| Biological source | Rattus norvegicus, Homo sapiens (Norway rat, human) |
| Cellular location | Cytoplasm, cytoskeleton (By similarity): O08816 |
| Total number of polymer chains | 1 |
| Total formula weight | 17422.83 |
| Authors | Volkman, B.F.,Prehoda, K.E.,Scott, J.A.,Peterson, F.C.,Lim, W.A. (deposition date: 2002-08-29, release date: 2002-12-04, Last modification date: 2024-05-22) |
| Primary citation | Volkman, B.F.,Prehoda, K.E.,Scott, J.A.,Peterson, F.C.,Lim, W.A. Structure of the N-WASP EVH1 Domain-WIP Complex. Insight into the Molecular Basis of Wiskott-Aldrich Syndrome. Cell(Cambridge,Mass.), 111:565-576, 2002 Cited by PubMed Abstract: Missense mutants that cause the immune disorder Wiskott-Aldrich Syndrome (WAS) map primarily to the Enabled/VASP homology 1 (EVH1) domain of the actin regulatory protein WASP. This domain has been implicated in both peptide and phospholipid binding. We show here that the N-WASP EVH1 domain does not bind phosphatidyl inositol-(4,5)-bisphosphate, as previously reported, but does specifically bind a 25 residue motif from the WASP Interacting Protein (WIP). The NMR structure of the complex reveals a novel recognition mechanism-the WIP ligand, which is far longer than canonical EVH1 ligands, wraps around the domain, contacting a narrow but extended surface. This recognition mechanism provides a basis for understanding the effects of mutations that cause WAS. PubMed: 12437929DOI: 10.1016/S0092-8674(02)01076-0 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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