1iap: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==CRYSTAL STRUCTURE OF P115RHOGEF RGRGS DOMAIN== | ==CRYSTAL STRUCTURE OF P115RHOGEF RGRGS DOMAIN== | ||
<StructureSection load='1iap' size='340' side='right' caption='[[1iap]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1iap' size='340' side='right'caption='[[1iap]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1iap]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IAP FirstGlance]. <br> | <table><tr><td colspan='2'>[[1iap]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IAP FirstGlance]. <br> | ||
| Line 28: | Line 28: | ||
</div> | </div> | ||
<div class="pdbe-citations 1iap" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1iap" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Rho guanine nucleotide exchange factor|Rho guanine nucleotide exchange factor]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 33: | Line 36: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Chen, Z]] | [[Category: Chen, Z]] | ||
[[Category: Sprang, S R]] | [[Category: Sprang, S R]] | ||
[[Category: P115]] | [[Category: P115]] | ||
[[Category: Rg]] | |||
[[Category: Rgrg]] | [[Category: Rgrg]] | ||
[[Category: Rhogef]] | [[Category: Rhogef]] | ||
[[Category: Signaling protein]] | [[Category: Signaling protein]] | ||
Revision as of 13:13, 30 October 2019
CRYSTAL STRUCTURE OF P115RHOGEF RGRGS DOMAINCRYSTAL STRUCTURE OF P115RHOGEF RGRGS DOMAIN
Structural highlights
Function[ARHG1_HUMAN] Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits. Acts as GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase. Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain. This GEF activity is inhibited by binding to activated GNA12. Mediates angiotensin-2-induced RhoA activation.[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 PubMedp115RhoGEF, a guanine nucleotide exchange factor for Rho GTPase, is also a GTPase activating protein (GAP) for G(12) and G(13) heterotrimeric G alpha subunits. Near its N-terminus, p115RhoGEF contains a domain (rgRGS) with remote sequence identity to RGS (regulators of G protein signaling) domains. The rgRGS domain is necessary but not sufficient for the GAP activity of p115RhoGEF. The 1.9 A resolution crystal structure of the rgRGS domain shows structural similarity to RGS domains but possesses a C-terminal extension that folds into a layer of helices that pack against the hydrophobic core of the domain. Mutagenesis experiments show that rgRGS may form interactions with G alpha(13) that are analogous to those in complexes of RGS proteins with their G alpha substrates. Structure of the rgRGS domain of p115RhoGEF.,Chen Z, Wells CD, Sternweis PC, Sprang SR Nat Struct Biol. 2001 Sep;8(9):805-9. PMID:11524686[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||