1mke

From Proteopedia

(Difference between revisions)

Current revision

Structure of the N-WASP EVH1 Domain-WIP complex

Structural highlights

1mke is a 1 chain structure with sequence from Homo sapiens and Rattus norvegicus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

WASL_RAT Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Involved in various processes, such as mitosis and cytokinesis, via its role in the regulation of actin polymerization. Together with CDC42, involved in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. In addition to its role in the cytoplasm, also plays a role in the nucleus by regulating gene transcription, probably by promoting nuclear actin polymerization (By similarity). Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. Plays a role in dendrite spine morphogenesis (By similarity).[UniProtKB:O00401][UniProtKB:Q91YD9]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Volkman BF, Prehoda KE, Scott JA, Peterson FC, Lim WA. Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich Syndrome. Cell. 2002 Nov 15;111(4):565-76. PMID:12437929

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mke"

@@ Line 1: / Line 1: @@
 ==Structure of the N-WASP EVH1 Domain-WIP complex==
-<StructureSection load='1mke' size='340' side='right'caption='[[1mke]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
+<StructureSection load='1mke' size='340' side='right'caption='[[1mke]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mke]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MKE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mke]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MKE FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mke OCA], [http://pdbe.org/1mke PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mke RCSB], [http://www.ebi.ac.uk/pdbsum/1mke PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mke ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mke OCA], [https://pdbe.org/1mke PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mke RCSB], [https://www.ebi.ac.uk/pdbsum/1mke PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mke ProSAT]</span></td></tr>
 </table>
-== Disease ==
-[[http://www.uniprot.org/uniprot/WIPF1_HUMAN WIPF1_HUMAN]] Defects in WIPF1 are the cause of Wiskott-Aldrich syndrome type 2 (WAS2) [MIM:[http://omim.org/entry/614493 614493]]. WAS2 is an immunodeficiency disorder characterized by eczema, thrombocytopenia, recurrent infections, defective T-cell proliferation, and impaired natural killer cell function.<ref>PMID:22231303</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/WIPF1_HUMAN WIPF1_HUMAN]] May have direct activity on the actin cytoskeleton. Induces actin polymerization and redistribution. Contributes with NCK1 and GRB2 in the recruitment and activation of WASL. May participate in regulating the subcellular localization of WASL, resulting in the disassembly of stress fibers in favor of filopodia formation (By similarity). Plays an important role in the intracellular motility of vaccinia virus by functioning as an adapter for recruiting WASL to vaccinia virus.<ref>PMID:9405671</ref> <ref>PMID:10878810</ref>
+[https://www.uniprot.org/uniprot/WASL_RAT WASL_RAT] Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Involved in various processes, such as mitosis and cytokinesis, via its role in the regulation of actin polymerization. Together with CDC42, involved in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. In addition to its role in the cytoplasm, also plays a role in the nucleus by regulating gene transcription, probably by promoting nuclear actin polymerization (By similarity). Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. Plays a role in dendrite spine morphogenesis (By similarity).[UniProtKB:O00401][UniProtKB:Q91YD9]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 30: @@
 ==See Also==
-*[[Wiskott-Aldrich syndrome protein|Wiskott-Aldrich syndrome protein]]
+*[[Wiskott-Aldrich syndrome protein 3D structures|Wiskott-Aldrich syndrome protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Lim, W A]]
+[[Category: Rattus norvegicus]]
-[[Category: Peterson, F C]]
+[[Category: Lim WA]]
-[[Category: Prehoda, K E]]
+[[Category: Peterson FC]]
-[[Category: Scott, J A]]
+[[Category: Prehoda KE]]
-[[Category: Volkman, B F]]
+[[Category: Scott JA]]
-[[Category: Polyproline]]
+[[Category: Volkman BF]]
-[[Category: Protein binding]]
-[[Category: Protein-protein complex]]

1mke

From Proteopedia

Current revision

Structure of the N-WASP EVH1 Domain-WIP complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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