1mke
From Proteopedia
(New page: 200px<br /><applet load="1mke" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mke" /> '''Structure of the N-WASP EVH1 Domain-WIP comp...) |
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| - | [[Image:1mke.jpg|left|200px]]<br /><applet load="1mke" size=" | + | [[Image:1mke.jpg|left|200px]]<br /><applet load="1mke" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mke" /> | caption="1mke" /> | ||
'''Structure of the N-WASP EVH1 Domain-WIP complex'''<br /> | '''Structure of the N-WASP EVH1 Domain-WIP complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Missense mutants that cause the immune disorder Wiskott-Aldrich Syndrome | + | 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== | ==About this Structure== | ||
| - | 1MKE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1MKE is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: ]] | [[Category: ]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Lim, W | + | [[Category: Lim, W A.]] |
| - | [[Category: Peterson, F | + | [[Category: Peterson, F C.]] |
| - | [[Category: Prehoda, K | + | [[Category: Prehoda, K E.]] |
| - | [[Category: Scott, J | + | [[Category: Scott, J A.]] |
| - | [[Category: Volkman, B | + | [[Category: Volkman, B F.]] |
[[Category: nmr]] | [[Category: nmr]] | ||
[[Category: polyproline]] | [[Category: polyproline]] | ||
[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:10 2008'' |
Revision as of 11:56, 21 February 2008
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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 Feb 21 13:56:10 2008
