6pcv: Difference between revisions

<table><tr><td colspan='2'>[[6pcv]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PCV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PCV FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PREX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), GNB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN]), GNG2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</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=6pcv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pcv OCA], [http://pdbe.org/6pcv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pcv RCSB], [http://www.ebi.ac.uk/pdbsum/6pcv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pcv ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/GBG2_BOVIN GBG2_BOVIN]] Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. [[http://www.uniprot.org/uniprot/GBB1_BOVIN GBB1_BOVIN]] Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.  

PIP3-dependent Rac exchanger 1 (P-Rex1) is activated downstream of G protein-coupled receptors to promote neutrophil migration and metastasis. The structure of more than half of the enzyme and its regulatory G protein binding site are unknown. Our 3.2 A cryo-EM structure of the P-Rex1-Gbetagamma complex reveals that the carboxyl-terminal half of P-Rex1 adopts a complex fold most similar to those of Legionella phosphoinositide phosphatases. Although catalytically inert, the domain coalesces with a DEP domain and two PDZ domains to form an extensive docking site for Gbetagamma. Hydrogen-deuterium exchange mass spectrometry suggests that Gbetagamma binding induces allosteric changes in P-Rex1, but functional assays indicate that membrane localization is also required for full activation. Thus, a multidomain assembly is key to the regulation of P-Rex1 by Gbetagamma and the formation of a membrane-localized scaffold optimized for recruitment of other signaling proteins such as PKA and PTEN.

 

Cryo-electron microscopy structure and analysis of the P-Rex1-Gbetagamma signaling scaffold.,Cash JN, Urata S, Li S, Ravala SK, Avramova LV, Shost MD, Gutkind JS, Tesmer JJG, Cianfrocco MA Sci Adv. 2019 Oct 16;5(10):eaax8855. doi: 10.1126/sciadv.aax8855. eCollection, 2019 Oct. PMID:31663027<ref>PMID:31663027</ref>

 

[[Category: Bovin]]

[[Category: Human]]

[[Category: Cash, J N]]

[[Category: Cianfrocco, M A]]

[[Category: Tesmer, J J.G]]

[[Category: Signaling protein]]