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2k2r

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Revision as of 04:47, 25 December 2014

The NMR structure of alpha-parvin CH2/paxillin LD1 complex

Structural highlights

2k2r is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	PARVA (Homo sapiens)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[PARVA_HUMAN] Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells to endothelial cells during blood vessel development (By similarity). Plays a role in the reorganization of the actin cytoskeleton, formation of lamellipodia and ciliogenesis. Plays a role in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration.^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Alpha-parvin is an essential component of focal adhesions (FAs), which are large multiprotein complexes that link the plasma membrane and actin cytoskeleton. Alpha-parvin contains two calponin homology (CH) domains and its C-terminal CH2 domain binds multiple targets including paxillin LD motifs for regulating the FA network and signaling. Here we describe the solution structure of alpha-parvin CH2 bound to paxillin LD1. We show that although CH2 contains the canonical CH-fold, a previously defined N-terminal linker forms an alpha-helix that packs unexpectedly with the C-terminal helix of CH2, resulting in a novel variant of the CH domain. Importantly, such packing generates a hydrophobic surface that recognizes the Leu-rich face of paxillin-LD1, and the binding pattern differs drastically from the classical paxillin-LD binding to four-helix bundle proteins such as focal adhesion kinase. These results define a novel modular recognition mode and reveal how alpha-parvin associates with paxillin to mediate the FA assembly and signaling.

The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel modular recognition for focal adhesion assembly.,Wang X, Fukuda K, Byeon IJ, Velyvis A, Wu C, Gronenborn A, Qin J J Biol Chem. 2008 Jul 25;283(30):21113-9. Epub 2008 May 28. PMID:18508764^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tu Y, Huang Y, Zhang Y, Hua Y, Wu C. A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading. J Cell Biol. 2001 Apr 30;153(3):585-98. PMID:11331308
↑ Nikolopoulos SN, Turner CE. Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion. J Cell Biol. 2000 Dec 25;151(7):1435-48. PMID:11134073
↑ Zhang Y, Chen K, Tu Y, Wu C. Distinct roles of two structurally closely related focal adhesion proteins, alpha-parvins and beta-parvins, in regulation of cell morphology and survival. J Biol Chem. 2004 Oct 1;279(40):41695-705. Epub 2004 Jul 28. PMID:15284246 doi:10.1074/jbc.M401563200
↑ Kim J, Lee JE, Heynen-Genel S, Suyama E, Ono K, Lee K, Ideker T, Aza-Blanc P, Gleeson JG. Functional genomic screen for modulators of ciliogenesis and cilium length. Nature. 2010 Apr 15;464(7291):1048-51. doi: 10.1038/nature08895. PMID:20393563 doi:10.1038/nature08895
↑ Wang X, Fukuda K, Byeon IJ, Velyvis A, Wu C, Gronenborn A, Qin J. The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel modular recognition for focal adhesion assembly. J Biol Chem. 2008 Jul 25;283(30):21113-9. Epub 2008 May 28. PMID:18508764 doi:10.1074/jbc.M801270200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2k2r"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2k2r]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K2R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K2R FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PARVA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PARVA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k2r RCSB], [http://www.ebi.ac.uk/pdbsum/2k2r PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k2r RCSB], [http://www.ebi.ac.uk/pdbsum/2k2r PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/PARVA_HUMAN PARVA_HUMAN]] Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells to endothelial cells during blood vessel development (By similarity). Plays a role in the reorganization of the actin cytoskeleton, formation of lamellipodia and ciliogenesis. Plays a role in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration.<ref>PMID:11331308</ref> <ref>PMID:11134073</ref> <ref>PMID:15284246</ref> <ref>PMID:20393563</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 34: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Byeon, I.]]
+[[Category: Byeon, I]]
-[[Category: Fukuda, K.]]
+[[Category: Fukuda, K]]
-[[Category: Gronenborn, A.]]
+[[Category: Gronenborn, A]]
-[[Category: Qin, J.]]
+[[Category: Qin, J]]
-[[Category: Velyvis, A.]]
+[[Category: Velyvis, A]]
-[[Category: Wang, X.]]
+[[Category: Wang, X]]
-[[Category: Wu, C.]]
+[[Category: Wu, C]]
 [[Category: Actin-binding]]
 [[Category: Cell adhesion]]

2k2r

From Proteopedia

Revision as of 04:47, 25 December 2014

The NMR structure of alpha-parvin CH2/paxillin LD1 complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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