1ow6: Difference between revisions

Revision as of 15:22, 21 February 2008

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

OverviewOverview

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 StructureAbout this Structure

1OW6 is a Single protein structure of sequence from Homo sapiens. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.

ReferenceReference

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 Thu Feb 21 14:22:16 2008

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OCA

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 ==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.
+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==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Transferase]]
-[[Category: Arold, S.T.]]
+[[Category: Arold, S T.]]
-[[Category: Campbell, I.D.]]
+[[Category: Campbell, I D.]]
-[[Category: Hoellerer, M.K.]]
+[[Category: Hoellerer, M K.]]
 [[Category: Labesse, G.]]
-[[Category: Noble, M.E.M.]]
+[[Category: Noble, M E.M.]]
-[[Category: Werner, J.M.]]
+[[Category: Werner, J M.]]
 [[Category: 4 helical bundle]]
 [[Category: amphiphatic helix]]
 [[Category: domain swapping]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:36:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:16 2008''