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1t01

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(New page: 200px<br /><applet load="1t01" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t01, resolution 2.06&Aring;" /> '''Vinculin complexed w...)
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[[Image:1t01.gif|left|200px]]<br /><applet load="1t01" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1t01, resolution 2.06&Aring;" />
'''Vinculin complexed with the VBS1 helix from talin'''<br />
'''Vinculin complexed with the VBS1 helix from talin'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1T01 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T01 OCA].
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1T01 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T01 OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[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.]]
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[[Category: Gingras, A.R.]]
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[[Category: Gingras, A R.]]
[[Category: Papagrigoriou, E.]]
[[Category: Papagrigoriou, E.]]
[[Category: five helix bundle]]
[[Category: five helix bundle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:53:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:12 2008''

Revision as of 13:08, 21 February 2008


1t01, resolution 2.06Å

Drag the structure with the mouse to rotate

Vinculin complexed with the VBS1 helix from talin

Overview

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.

About this Structure

1T01 is a Protein complex structure of sequences from Gallus gallus and Mus musculus. Full crystallographic information is available from OCA.

Reference

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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