1u89
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1sj7|1SJ7]], [[1sj8|1SJ8]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u89 OCA], [http://www.ebi.ac.uk/pdbsum/1u89 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u89 RCSB]</span> | ||
}} | }} | ||
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[[Category: left-handed]] | [[Category: left-handed]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:06:41 2008'' |
Revision as of 21:06, 30 March 2008
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Related: | 1SJ7, 1SJ8
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Solution structure of VBS2 fragment of talin
Overview
The cytoskeletal protein talin plays a key role in activating integrins and in coupling them to the actin cytoskeleton. Its N-terminal globular head, which binds beta integrins, is linked to an extended rod having a C-terminal actin binding site and several vinculin binding sites (VBSs). The NMR structure of residues 755-889 of the rod (containing a VBS) is shown to be an amphipathic four-helix bundle with a left-handed topology. A talin peptide corresponding to the VBS binds the vinculin head; the X-ray crystallographic structure of this complex shows that the residues which interact with vinculin are buried in the hydrophobic core of the talin fragment. NMR shows that the interaction involves a major structural change in the talin fragment, including unfolding of one of its helices, making the VBS accessible to vinculin. Interestingly, the talin 755-889 fragment binds more than one vinculin head molecule, suggesting that the talin rod may contain additional as yet unrecognized VBSs.
About this Structure
1U89 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head., Fillingham I, Gingras AR, Papagrigoriou E, Patel B, Emsley J, Critchley DR, Roberts GC, Barsukov IL, Structure. 2005 Jan;13(1):65-74. PMID:15642262
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