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1mke
From Proteopedia
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| - | [[Image:1mke.jpg|left|200px]] | + | [[Image:1mke.jpg|left|200px]] |
| - | + | ||
| - | '''Structure of the N-WASP EVH1 Domain-WIP complex''' | + | {{Structure |
| + | |PDB= 1mke |SIZE=350|CAPTION= <scene name='initialview01'>1mke</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of the N-WASP EVH1 Domain-WIP complex''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MKE is a [ | + | 1MKE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKE OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich Syndrome., Volkman BF, Prehoda KE, Scott JA, Peterson FC, Lim WA, Cell. 2002 Nov 15;111(4):565-76. PMID:[http:// | + | Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich Syndrome., Volkman BF, Prehoda KE, Scott JA, Peterson FC, Lim WA, Cell. 2002 Nov 15;111(4):565-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12437929 12437929] |
[[Category: ]] | [[Category: ]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:44:30 2008'' |
Revision as of 10:44, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the N-WASP EVH1 Domain-WIP complex
Overview
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.
About this Structure
1MKE is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich Syndrome., Volkman BF, Prehoda KE, Scott JA, Peterson FC, Lim WA, Cell. 2002 Nov 15;111(4):565-76. PMID:12437929 [[Category: ]]
Page seeded by OCA on Thu Mar 20 12:44:30 2008
