1u89: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
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...
 
No edit summary
Line 1: Line 1:
[[Image:1u89.gif|left|200px]]<br /><applet load="1u89" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1u89.gif|left|200px]]<br /><applet load="1u89" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1u89" />
caption="1u89" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U89 OCA].  
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==
Line 13: Line 13:
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Barsukov, I.L.]]
[[Category: Barsukov, I L.]]
[[Category: Critchley, D.R.]]
[[Category: Critchley, D R.]]
[[Category: Emsley, J.]]
[[Category: Emsley, J.]]
[[Category: Fillingham, I.]]
[[Category: Fillingham, I.]]
[[Category: Gingras, A.R.]]
[[Category: Gingras, A R.]]
[[Category: Papagrigoriou, E.]]
[[Category: Papagrigoriou, E.]]
[[Category: Patel, B.]]
[[Category: Patel, B.]]
[[Category: Roberts, G.C.K.]]
[[Category: Roberts, G C.K.]]
[[Category: 4-helix bundle]]
[[Category: 4-helix bundle]]
[[Category: left-handed]]
[[Category: left-handed]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:55:12 2007''
''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

File:1u89.gif


1u89

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Thu Feb 21 15:21:35 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA