1ow7

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[[Image:1ow7.jpg|left|200px]]
[[Image:1ow7.jpg|left|200px]]
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{{Structure
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|PDB= 1ow7 |SIZE=350|CAPTION= <scene name='initialview01'>1ow7</scene>, resolution 2.60&Aring;
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The line below this paragraph, containing "STRUCTURE_1ow7", creates the "Structure Box" on the page.
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] </span>
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|GENE= PTK2 OR FAK1 OR FAK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1ow7| PDB=1ow7 | SCENE= }}
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|RELATEDENTRY=[[1k05|1K05]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ow7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ow7 OCA], [http://www.ebi.ac.uk/pdbsum/1ow7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ow7 RCSB]</span>
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'''Paxillin LD4 motif bound to the Focal Adhesion Targeting (FAT) domain of the Focal Adhesion Kinase'''
'''Paxillin LD4 motif bound to the Focal Adhesion Targeting (FAT) domain of the Focal Adhesion Kinase'''
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[[Category: Werner, J M.]]
[[Category: Werner, J M.]]
[[Category: 4 helical bundle]]
[[Category: 4 helical bundle]]
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[[Category: amphiphatic helix]]
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[[Category: Amphiphatic helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:21:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:51:12 2008''
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Revision as of 01:21, 3 May 2008

Template:STRUCTURE 1ow7

Paxillin LD4 motif bound to the Focal Adhesion Targeting (FAT) domain of the Focal Adhesion Kinase


Overview

Focal adhesions (FAs) are large submembrane signaling complexes formed at sites of cellular attachment to the extracellular matrix. The interaction of LD motifs with their targets plays an important role in the assembly of FAs. We have determined the molecular basis for the recognition of two paxillin LD motifs by the FA targeting (FAT) domain of FA kinase using a combination of X-ray crystallography, solution NMR, and homology modeling. The four-helix FAT domain displays two LD binding sites on opposite sites of the molecule that bind LD peptides in a helical conformation. Threading studies suggest that the LD-interacting domain of p95PKL shares a common four-helical core with the FAT domain and the tail of vinculin, defining a structural family of LD motif binding modules.

About this Structure

1OW7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Molecular recognition of paxillin LD motifs by the focal adhesion targeting domain., Hoellerer MK, Noble ME, Labesse G, Campbell ID, Werner JM, Arold ST, Structure. 2003 Oct;11(10):1207-17. PMID:14527389 Page seeded by OCA on Sat May 3 04:21:00 2008

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