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http://purl.uniprot.org/citations/17690686http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17690686http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17690686http://www.w3.org/2000/01/rdf-schema#comment"Human filamins are large actin-crosslinking proteins composed of an N-terminal actin-binding domain followed by 24 Ig-like domains (IgFLNs), which interact with numerous transmembrane receptors and cytosolic signaling proteins. Here we report the 2.5 A resolution structure of a three-domain fragment of human filamin A (IgFLNa19-21). The structure reveals an unexpected domain arrangement, with IgFLNa20 partially unfolded bringing IgFLNa21 into close proximity to IgFLNa19. Notably the N-terminus of IgFLNa20 forms a beta-strand that associates with the CD face of IgFLNa21 and occupies the binding site for integrin adhesion receptors. Disruption of this IgFLNa20-IgFLNa21 interaction enhances filamin binding to integrin beta-tails. Structural and functional analysis of other IgFLN domains suggests that auto-inhibition by adjacent IgFLN domains may be a general mechanism controlling filamin-ligand interactions. This can explain the increased integrin binding of filamin splice variants and provides a mechanism by which ligand binding might impact filamin structure."xsd:string
http://purl.uniprot.org/citations/17690686http://purl.org/dc/terms/identifier"doi:10.1038/sj.emboj.7601827"xsd:string
http://purl.uniprot.org/citations/17690686http://purl.org/dc/terms/identifier"doi:10.1038/sj.emboj.7601827"xsd:string
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/author"Jiang P."xsd:string
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/author"Jiang P."xsd:string
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/author"Kiema T."xsd:string
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/author"Kiema T."xsd:string
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/author"Calderwood D.A."xsd:string
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/author"Calderwood D.A."xsd:string
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/author"Ylanne J."xsd:string
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/author"Ylanne J."xsd:string
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/author"Campbell I.D."xsd:string
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/author"Campbell I.D."xsd:string
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/author"Lad Y."xsd:string
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/author"Lad Y."xsd:string
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/author"Coles C.H."xsd:string
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/author"Coles C.H."xsd:string
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/author"Pentikainen O.T."xsd:string
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/author"Pentikainen O.T."xsd:string
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/17690686http://purl.uniprot.org/core/name"EMBO J."xsd:string