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http://purl.uniprot.org/citations/12437929http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12437929http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12437929http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/12437929http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(02)01076-0"xsd:string
http://purl.uniprot.org/citations/12437929http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(02)01076-0"xsd:string
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/author"Lim W.A."xsd:string
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/author"Lim W.A."xsd:string
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/author"Scott J.A."xsd:string
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/author"Scott J.A."xsd:string
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/author"Peterson F.C."xsd:string
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/author"Peterson F.C."xsd:string
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/author"Volkman B.F."xsd:string
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/author"Volkman B.F."xsd:string
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/author"Prehoda K.E."xsd:string
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/author"Prehoda K.E."xsd:string
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/pages"565-576"xsd:string
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/pages"565-576"xsd:string
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/title"Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich Syndrome."xsd:string
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/title"Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich Syndrome."xsd:string
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/volume"111"xsd:string
http://purl.uniprot.org/citations/12437929http://purl.uniprot.org/core/volume"111"xsd:string