1sj8: Difference between revisions

Revision as of 13:44, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1sj8.png

Template:STRUCTURE 1sj8

Crystal Structure of talin residues 482-789Crystal Structure of talin residues 482-789

Template:ABSTRACT PUBMED 15272303

About this StructureAbout this Structure

1SJ8 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle., Papagrigoriou E, Gingras AR, Barsukov IL, Bate N, Fillingham IJ, Patel B, Frank R, Ziegler WH, Roberts GC, Critchley DR, Emsley J, EMBO J. 2004 Aug 4;23(15):2942-51. Epub 2004 Jul 22. PMID:15272303

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OCA

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-'''Crystal Structure of talin residues 482-789'''
+===Crystal Structure of talin residues 482-789===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15272303}}, adds the Publication Abstract to the page
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 [[Category: Papagrigoriou, E.]]
 [[Category: Structural protein]]
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