1u89
From Proteopedia
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[[Image:1u89.gif|left|200px]] | [[Image:1u89.gif|left|200px]] | ||
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'''Solution structure of VBS2 fragment of talin''' | '''Solution structure of VBS2 fragment of talin''' | ||
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[[Category: Roberts, G C.K.]] | [[Category: Roberts, G C.K.]] | ||
[[Category: 4-helix bundle]] | [[Category: 4-helix bundle]] | ||
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Revision as of 07:53, 3 May 2008
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 Page seeded by OCA on Sat May 3 10:53:12 2008