1zw2: Difference between revisions
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'''Vinculin Head (0-258) in Complex with the Talin Rod residues 2345-2369''' | {{Structure | ||
|PDB= 1zw2 |SIZE=350|CAPTION= <scene name='initialview01'>1zw2</scene>, resolution 2.10Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= VCL, VINC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus]) | |||
}} | |||
'''Vinculin Head (0-258) in Complex with the Talin Rod residues 2345-2369''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ZW2 is a [ | 1ZW2 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZW2 OCA]. | ||
==Reference== | ==Reference== | ||
Mapping and consensus sequence identification for multiple vinculin binding sites within the talin rod., Gingras AR, Ziegler WH, Frank R, Barsukov IL, Roberts GC, Critchley DR, Emsley J, J Biol Chem. 2005 Nov 4;280(44):37217-24. Epub 2005 Aug 30. PMID:[http:// | Mapping and consensus sequence identification for multiple vinculin binding sites within the talin rod., Gingras AR, Ziegler WH, Frank R, Barsukov IL, Roberts GC, Critchley DR, Emsley J, J Biol Chem. 2005 Nov 4;280(44):37217-24. Epub 2005 Aug 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16135522 16135522] | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: vinculin]] | [[Category: vinculin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:40:30 2008'' | ||
Revision as of 16:40, 20 March 2008
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| , resolution 2.10Å | |||||||
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| Gene: | VCL, VINC1 (Gallus gallus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Vinculin Head (0-258) in Complex with the Talin Rod residues 2345-2369
OverviewOverview
The interaction between the cytoskeletal proteins talin and vinculin plays a key role in integrin-mediated cell adhesion and migration. Three vinculin binding sites (VBS1-3) have previously been identified in the talin rod using a yeast two-hybrid assay. To extend these studies, we spot-synthesized a series of peptides spanning all the alpha-helical regions predicted for the talin rod and identified eight additional VBSs, two of which overlap key functional regions of the rod, including the integrin binding site and C-terminal actin binding site. The talin VBS alpha-helices bind to a hydrophobic cleft in the N-terminal vinculin Vd1 domain. We have defined the specificity of this interaction by spot-synthesizing a series of 25-mer talin VBS1 peptides containing substitutions with all the commonly occurring amino acids. The consensus for recognition is LXXAAXXVAXX- VXXLIXXA with distinct classes of hydrophobic side chains at positions 1, 4, 5, 8, 9, 12, 15, and 16 required for vinculin binding. Positions 1, 8, 12, 15, and 16 require an aliphatic residue and will not tolerate alanine, whereas positions 4, 5, and 9 are less restrictive. These preferences are common to all 11 VBS sequences with a minor variation occurring in one case. A crystal structure of this variant VBS peptide in complex with the vinculin Vd1 domain reveals a subtly different mode of vinculin binding.
About this StructureAbout this Structure
1ZW2 is a Protein complex structure of sequences from Gallus gallus. Full crystallographic information is available from OCA.
ReferenceReference
Mapping and consensus sequence identification for multiple vinculin binding sites within the talin rod., Gingras AR, Ziegler WH, Frank R, Barsukov IL, Roberts GC, Critchley DR, Emsley J, J Biol Chem. 2005 Nov 4;280(44):37217-24. Epub 2005 Aug 30. PMID:16135522
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