Molecular recognition of paxillin LD motifs by the focal adhesion targeting domain
Molecular recognition of paxillin LD motifs by the focal adhesion targeting domain
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 adhesion, structure, FAK, paxillin, interaction, NMR, x-ray
1207-1217
Hoellerer, Maria K.
dcaa8758-3e52-42bc-a06a-6482b24512a7
Noble, Martin E.M.
8afd7343-e122-48d1-a44a-1ee7be56d774
Labesse, Gilles
3ce9bb36-6b85-4198-b33c-cab284077ffc
Campbell, Iain D.
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Werner, Jörn M.
1b02513a-8310-4f4f-adac-dc2a466bd115
Arold, Stefan T.
2dcaea11-64b4-4298-9faa-d70708fc4df7
October 2003
Hoellerer, Maria K.
dcaa8758-3e52-42bc-a06a-6482b24512a7
Noble, Martin E.M.
8afd7343-e122-48d1-a44a-1ee7be56d774
Labesse, Gilles
3ce9bb36-6b85-4198-b33c-cab284077ffc
Campbell, Iain D.
54eba33e-94f7-450e-b555-c429dc2179de
Werner, Jörn M.
1b02513a-8310-4f4f-adac-dc2a466bd115
Arold, Stefan T.
2dcaea11-64b4-4298-9faa-d70708fc4df7
Hoellerer, Maria K., Noble, Martin E.M., Labesse, Gilles, Campbell, Iain D., Werner, Jörn M. and Arold, Stefan T.
(2003)
Molecular recognition of paxillin LD motifs by the focal adhesion targeting domain.
Structure, 11 (10), .
(doi:10.1016/j.str.2003.08.010).
Abstract
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.
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Submitted date: February 2003
Published date: October 2003
Keywords:
focal adhesion, structure, FAK, paxillin, interaction, NMR, x-ray
Identifiers
Local EPrints ID: 40775
URI: http://eprints.soton.ac.uk/id/eprint/40775
ISSN: 0969-2126
PURE UUID: 70cfcfe7-cbb1-4f67-8180-00f970fc996b
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Date deposited: 10 Jul 2006
Last modified: 16 Mar 2024 03:36
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Contributors
Author:
Maria K. Hoellerer
Author:
Martin E.M. Noble
Author:
Gilles Labesse
Author:
Iain D. Campbell
Author:
Stefan T. Arold
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