1nyp
From Proteopedia
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| - | [[Image:1nyp.gif|left|200px]] | + | [[Image:1nyp.gif|left|200px]] |
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| - | '''4th LIM domain of PINCH protein''' | + | {{Structure |
| + | |PDB= 1nyp |SIZE=350|CAPTION= <scene name='initialview01'>1nyp</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= LIMS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''4th LIM domain of PINCH protein''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NYP is a [ | + | 1NYP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NYP OCA]. |
==Reference== | ==Reference== | ||
| - | Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling., Velyvis A, Vaynberg J, Yang Y, Vinogradova O, Zhang Y, Wu C, Qin J, Nat Struct Biol. 2003 Jul;10(7):558-64. PMID:[http:// | + | Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling., Velyvis A, Vaynberg J, Yang Y, Vinogradova O, Zhang Y, Wu C, Qin J, Nat Struct Biol. 2003 Jul;10(7):558-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12794636 12794636] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protein recognition]] | [[Category: protein recognition]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:03:26 2008'' |
Revision as of 11:03, 20 March 2008
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| Ligands: | |||||||
| Gene: | LIMS1 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
4th LIM domain of PINCH protein
Overview
PINCH is an adaptor protein found in focal adhesions, large cellular complexes that link extracellular matrix to the actin cytoskeleton. PINCH, which contains an array of five LIM domains, has been implicated as a platform for multiple protein-protein interactions that mediate integrin signaling within focal adhesions. We had previously characterized the LIM1 domain of PINCH, which functions in focal adhesions by binding specifically to integrin-linked kinase. Using NMR spectroscopy, we show here that the PINCH LIM4 domain, while maintaining the conserved LIM scaffold, recognizes the third SH3 domain of another adaptor protein, Nck2 (also called Nckbeta or Grb4), in a manner distinct from that of the LIM1 domain. Point mutation of LIM residues in the SH3-binding interface disrupted LIM-SH3 interaction and substantially impaired localization of PINCH to focal adhesions. These data provide novel structural insight into LIM domain-mediated protein-protein recognition and demonstrate that the PINCH-Nck2 interaction is an important component of the focal adhesion assembly during integrin signaling.
About this Structure
1NYP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling., Velyvis A, Vaynberg J, Yang Y, Vinogradova O, Zhang Y, Wu C, Qin J, Nat Struct Biol. 2003 Jul;10(7):558-64. PMID:12794636
Page seeded by OCA on Thu Mar 20 13:03:26 2008
Categories: Homo sapiens | Single protein | Qin, J. | Vaynberg, J. | Velyvis, A. | Vinogradova, O. | Wu, C. | Zhang, Y. | ZN | Lim domain | Protein recognition
