4edl

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[[Image:4edl.png|left|200px]]
 
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{{STRUCTURE_4edl| PDB=4edl | SCENE= }}
{{STRUCTURE_4edl| PDB=4edl | SCENE= }}
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===Crystal structure of beta-parvin CH2 domain===
===Crystal structure of beta-parvin CH2 domain===
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{{ABSTRACT_PUBMED_22869380}}
{{ABSTRACT_PUBMED_22869380}}
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==Function==
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[[http://www.uniprot.org/uniprot/PARVB_HUMAN PARVB_HUMAN]] Adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases CDC42 and RAC1 by guanine exchange factors, such as ARHGEF6. Is involved in the reorganization of the actin cytoskeleton and formation of lamellipodia. Plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration.<ref>PMID:11402068</ref> <ref>PMID:15005707</ref> <ref>PMID:15284246</ref> <ref>PMID:15159419</ref> <ref>PMID:18325335</ref>
==About this Structure==
==About this Structure==
[[4edl]] is a 6 chain structure with 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=4EDL OCA].
[[4edl]] is a 6 chain structure with 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=4EDL OCA].
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==Reference==
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<ref group="xtra">PMID:022869380</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Boggon, T J.]]
[[Category: Boggon, T J.]]

Revision as of 07:44, 20 June 2013

Template:STRUCTURE 4edl

Contents

Crystal structure of beta-parvin CH2 domain

Template:ABSTRACT PUBMED 22869380

Function

[PARVB_HUMAN] Adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases CDC42 and RAC1 by guanine exchange factors, such as ARHGEF6. Is involved in the reorganization of the actin cytoskeleton and formation of lamellipodia. Plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration.[1] [2] [3] [4] [5]

About this Structure

4edl is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Stiegler AL, Draheim KM, Li X, Chayen NE, Calderwood DA, Boggon TJ. Structural Basis for Paxillin Binding and Focal Adhesion Targeting of beta-Parvin. J Biol Chem. 2012 Sep 21;287(39):32566-77. Epub 2012 Aug 6. PMID:22869380 doi:10.1074/jbc.M112.367342
  1. Yamaji S, Suzuki A, Sugiyama Y, Koide Y, Yoshida M, Kanamori H, Mohri H, Ohno S, Ishigatsubo Y. A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction. J Cell Biol. 2001 Jun 11;153(6):1251-64. PMID:11402068
  2. Mishima W, Suzuki A, Yamaji S, Yoshimi R, Ueda A, Kaneko T, Tanaka J, Miwa Y, Ohno S, Ishigatsubo Y. The first CH domain of affixin activates Cdc42 and Rac1 through alphaPIX, a Cdc42/Rac1-specific guanine nucleotide exchanging factor. Genes Cells. 2004 Mar;9(3):193-204. PMID:15005707
  3. 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
  4. Yamaji S, Suzuki A, Kanamori H, Mishima W, Yoshimi R, Takasaki H, Takabayashi M, Fujimaki K, Fujisawa S, Ohno S, Ishigatsubo Y. Affixin interacts with alpha-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell-substrate interaction. J Cell Biol. 2004 May 24;165(4):539-51. PMID:15159419 doi:10.1083/jcb.200308141
  5. Matsuda C, Kameyama K, Suzuki A, Mishima W, Yamaji S, Okamoto H, Nishino I, Hayashi YK. Affixin activates Rac1 via betaPIX in C2C12 myoblast. FEBS Lett. 2008 Apr 9;582(8):1189-96. doi: 10.1016/j.febslet.2008.01.064. Epub, 2008 Mar 4. PMID:18325335 doi:10.1016/j.febslet.2008.01.064

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