1fgz

<table><tr><td colspan='2'>[[1fgz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FGZ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fgy|1fgy]]</div></td></tr>

[[https://www.uniprot.org/uniprot/CYH3_MOUSE CYH3_MOUSE]] Promotes guanine-nucleotide exchange on ARF1. Promotes the activation of ARF factors through replacement of GDP with GTP.<ref>PMID:18042453</ref>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Lipid second messengers generated by phosphoinositide (PI) 3-kinases regulate diverse cellular functions through interaction with pleckstrin homology (PH) domains in modular signaling proteins. The PH domain of Grp1, a PI 3-kinase-activated exchange factor for Arf GTPases, selectively binds phosphatidylinositol 3,4,5-trisphosphate with high affinity. We have determined the structure of the Grp1 PH domain in the unliganded form and bound to inositol 1,3,4,5-tetraphosphate. A novel mode of phosphoinositide recognition involving a 20-residue insertion within the beta6/beta7 loop explains the unusually high specificity of the Grp1 PH domain and the promiscuous 3-phosphoinositide binding typical of several PH domains including that of protein kinase B. When compared to other PH domains, general determinants of 3-phosphoinositide recognition and specificity can be deduced.

Structural basis of 3-phosphoinositide recognition by pleckstrin homology domains.,Lietzke SE, Bose S, Cronin T, Klarlund J, Chawla A, Czech MP, Lambright DG Mol Cell. 2000 Aug;6(2):385-94. PMID:10983985<ref>PMID:10983985</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1fgz" style="background-color:#fffaf0;"></div>

[[Category: Lk3 transgenic mice]]

[[Category: Bose, S]]

[[Category: Chawla, A]]

[[Category: Cronin, T]]

[[Category: Czech, M P]]

[[Category: Klarlund, J]]

[[Category: Lambright, D G]]

[[Category: Lietzke, S E]]

[[Category: Signaling protein]]