1sj8: Difference between revisions

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[[Image:1sj8.gif|left|200px]]<br /><applet load="1sj8" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1sj8.gif|left|200px]]
caption="1sj8, resolution 2.60&Aring;" />
 
'''Crystal Structure of talin residues 482-789'''<br />
{{Structure
|PDB= 1sj8 |SIZE=350|CAPTION= <scene name='initialview01'>1sj8</scene>, resolution 2.60&Aring;
|SITE=
|LIGAND=
|ACTIVITY=
|GENE= TLN1, TLN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
}}
 
'''Crystal Structure of talin residues 482-789'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1SJ8 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=1SJ8 OCA].  
1SJ8 is a [[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=1SJ8 OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15272303 15272303]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15272303 15272303]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: structural protein]]
[[Category: structural protein]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:02:02 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:05:38 2008''

Revision as of 15:05, 20 March 2008

File:1sj8.gif


PDB ID 1sj8

Drag the structure with the mouse to rotate
, resolution 2.60Å
Gene: TLN1, TLN (Mus musculus)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of talin residues 482-789


OverviewOverview

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 StructureAbout this Structure

1SJ8 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

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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