4gyv: Difference between revisions

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===Crystal strucure of the DH domain of FARP2===
===Crystal strucure of the DH domain of FARP2===
{{ABSTRACT_PUBMED_23375260}}
{{ABSTRACT_PUBMED_23375260}}
==Function==
[[http://www.uniprot.org/uniprot/FARP2_MOUSE FARP2_MOUSE]] Rho-guanine nucleotide exchange factor that activates RAC1. Plays a role in the response to class 3 semaphorins and remodeling of the actin cytoskeleton.<ref>PMID:12351724</ref><ref>PMID:16286926</ref>


==About this Structure==
==About this Structure==
[[4gyv]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYV OCA].  
[[4gyv]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYV OCA].  
==Reference==
<references group="xtra"/><references/>
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: He, X.]]
[[Category: He, X.]]

Revision as of 07:48, 27 March 2013

Template:STRUCTURE 4gyv

Crystal strucure of the DH domain of FARP2

Template:ABSTRACT PUBMED 23375260

Function

[FARP2_MOUSE] Rho-guanine nucleotide exchange factor that activates RAC1. Plays a role in the response to class 3 semaphorins and remodeling of the actin cytoskeleton.[1][2]

About this Structure

4gyv is a 9 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

  1. ↑ Kubo T, Yamashita T, Yamaguchi A, Sumimoto H, Hosokawa K, Tohyama M. A novel FERM domain including guanine nucleotide exchange factor is involved in Rac signaling and regulates neurite remodeling. J Neurosci. 2002 Oct 1;22(19):8504-13. PMID:12351724
  2. ↑ Toyofuku T, Yoshida J, Sugimoto T, Zhang H, Kumanogoh A, Hori M, Kikutani H. FARP2 triggers signals for Sema3A-mediated axonal repulsion. Nat Neurosci. 2005 Dec;8(12):1712-9. Epub 2005 Nov 13. PMID:16286926 doi:nn1596

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