1fgz: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(11 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:1fgz.png|left|200px]]


<!--
==GRP1 PH DOMAIN (UNLIGANDED)==
The line below this paragraph, containing "STRUCTURE_1fgz", creates the "Structure Box" on the page.
<StructureSection load='1fgz' size='340' side='right'caption='[[1fgz]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1fgz]] 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=1FGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FGZ FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_1fgz|  PDB=1fgz  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgz OCA], [https://pdbe.org/1fgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fgz RCSB], [https://www.ebi.ac.uk/pdbsum/1fgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fgz 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/1fgz_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=1fgz 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 (UNLIGANDED)===
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>
The line below this paragraph, {{ABSTRACT_PUBMED_10983985}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1fgz" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 10983985 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_10983985}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1FGZ is a 1 chain structure of 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=1FGZ OCA].
 
==Reference==
<ref group="xtra">PMID:10983985</ref><references group="xtra"/>
[[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]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 13:08:24 2009''

Latest revision as of 06:37, 30 October 2024

GRP1 PH DOMAIN (UNLIGANDED)

1fgz, resolution 2.05Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA