1fgy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:26, 6 November 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1fgy.png|left|200px]]
 
-
{{STRUCTURE_1fgy| PDB=1fgy | SCENE= }}
+
==GRP1 PH DOMAIN WITH INS(1,3,4,5)P4==
 +
<StructureSection load='1fgy' size='340' side='right'caption='[[1fgy]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1fgy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FGY FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4IP:INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE'>4IP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgy OCA], [https://pdbe.org/1fgy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fgy RCSB], [https://www.ebi.ac.uk/pdbsum/1fgy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fgy ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[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>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fg/1fgy_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fgy ConSurf].
 +
<div style="clear:both"></div>
 +
<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.
-
===GRP1 PH DOMAIN WITH INS(1,3,4,5)P4===
+
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>
-
{{ABSTRACT_PUBMED_10983985}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 1fgy" style="background-color:#fffaf0;"></div>
-
[[1fgy]] is a 1 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=1FGY OCA].
+
== References ==
-
 
+
<references/>
-
==Reference==
+
__TOC__
-
<ref group="xtra">PMID:010983985</ref><references group="xtra"/>
+
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Bose, S.]]
+
[[Category: Bose S]]
-
[[Category: Chawla, A.]]
+
[[Category: Chawla A]]
-
[[Category: Cronin, T.]]
+
[[Category: Cronin T]]
-
[[Category: Czech, M P.]]
+
[[Category: Czech MP]]
-
[[Category: Klarlund, J.]]
+
[[Category: Klarlund J]]
-
[[Category: Lambright, D G.]]
+
[[Category: Lambright DG]]
-
[[Category: Lietzke, S E.]]
+
[[Category: Lietzke SE]]
-
[[Category: Ph domain]]
+
-
[[Category: Signaling protein]]
+

Current revision

GRP1 PH DOMAIN WITH INS(1,3,4,5)P4

PDB ID 1fgy

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fgy"
Personal tools