1u6h

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(New page: 200px<br /><applet load="1u6h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u6h, resolution 2.38&Aring;" /> '''Vinculin head (0-258...)
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[[Image:1u6h.gif|left|200px]]<br /><applet load="1u6h" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1u6h.gif|left|200px]]<br /><applet load="1u6h" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1u6h, resolution 2.38&Aring;" />
caption="1u6h, resolution 2.38&Aring;" />
'''Vinculin head (0-258) in complex with the talin vinculin binding site 2 (849-879)'''<br />
'''Vinculin head (0-258) in complex with the talin vinculin binding site 2 (849-879)'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1U6H is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U6H OCA].
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1U6H is a [http://en.wikipedia.org/wiki/Protein_complex 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=1U6H OCA].
==Reference==
==Reference==
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Barsukov, I.L.]]
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[[Category: Barsukov, I L.]]
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[[Category: Critchley, D.R.]]
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[[Category: Critchley, D R.]]
[[Category: Emsley, J.]]
[[Category: Emsley, J.]]
[[Category: Fillingham, I.]]
[[Category: Fillingham, I.]]
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[[Category: Gingras, A.R.]]
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[[Category: Gingras, A R.]]
[[Category: Papagrigoriou, E.]]
[[Category: Papagrigoriou, E.]]
[[Category: Patel, B.]]
[[Category: Patel, B.]]
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[[Category: Roberts, G.C.K.]]
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[[Category: Roberts, G C.K.]]
[[Category: protein-protein complex]]
[[Category: protein-protein complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:52:43 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:21:05 2008''

Revision as of 13:21, 21 February 2008


1u6h, resolution 2.38Å

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Vinculin head (0-258) in complex with the talin vinculin binding site 2 (849-879)

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

1U6H is a Protein complex structure of sequences from Gallus gallus. 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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