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http://purl.uniprot.org/citations/15272303http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15272303http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15272303http://www.w3.org/2000/01/rdf-schema#comment"The interaction between the cytoskeletal proteins talin and vinculin plays a key role in integrin-mediated cell adhesion and migration. We have determined the crystal structures of two domains from the talin rod spanning residues 482-789. Talin 482-655, which contains a vinculin-binding site (VBS), folds into a five-helix bundle whereas talin 656-789 is a four-helix bundle. We show that the VBS is composed of a hydrophobic surface spanning five turns of helix 4. All the key side chains from the VBS are buried and contribute to the hydrophobic core of the talin 482-655 fold. We demonstrate that the talin 482-655 five-helix bundle represents an inactive conformation, and mutations that disrupt the hydrophobic core or deletion of helix 5 are required to induce an active conformation in which the VBS is exposed. We also report the crystal structure of the N-terminal vinculin head domain in complex with an activated form of talin. Activation of the VBS in talin and the recruitment of vinculin may support the maturation of small integrin/talin complexes into more stable adhesions."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.org/dc/terms/identifier"doi:10.1038/sj.emboj.7600285"xsd:string
http://purl.uniprot.org/citations/15272303http://purl.org/dc/terms/identifier"doi:10.1038/sj.emboj.7600285"xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Frank R."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Frank R."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Patel B."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Patel B."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Papagrigoriou E."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Papagrigoriou E."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Barsukov I.L."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Barsukov I.L."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Bate N."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Bate N."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Critchley D.R."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Critchley D.R."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Gingras A.R."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Gingras A.R."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Roberts G.C.K."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Roberts G.C.K."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Fillingham I.J."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Fillingham I.J."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Ziegler W.H."xsd:string
http://purl.uniprot.org/citations/15272303http://purl.uniprot.org/core/author"Ziegler W.H."xsd:string