1u89: Difference between revisions
New page: left|200px<br /><applet load="1u89" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u89" /> '''Solution structure of VBS2 fragment of talin... |
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'''Solution structure of VBS2 fragment of talin'''<br /> | '''Solution structure of VBS2 fragment of talin'''<br /> | ||
==Overview== | ==Overview== | ||
The cytoskeletal protein talin plays a key role in activating integrins | 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== | ||
1U89 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | 1U89 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U89 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Barsukov, I | [[Category: Barsukov, I L.]] | ||
[[Category: Critchley, D | [[Category: Critchley, D R.]] | ||
[[Category: Emsley, J.]] | [[Category: Emsley, J.]] | ||
[[Category: Fillingham, I.]] | [[Category: Fillingham, I.]] | ||
[[Category: Gingras, A | [[Category: Gingras, A R.]] | ||
[[Category: Papagrigoriou, E.]] | [[Category: Papagrigoriou, E.]] | ||
[[Category: Patel, B.]] | [[Category: Patel, B.]] | ||
[[Category: Roberts, G | [[Category: Roberts, G C.K.]] | ||
[[Category: 4-helix bundle]] | [[Category: 4-helix bundle]] | ||
[[Category: left-handed]] | [[Category: left-handed]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:21:35 2008'' |
Revision as of 16:21, 21 February 2008
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Solution structure of VBS2 fragment of talin
OverviewOverview
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 StructureAbout this Structure
1U89 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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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