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1fgy
From Proteopedia
(Difference between revisions)
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<StructureSection load='1fgy' size='340' side='right'caption='[[1fgy]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='1fgy' size='340' side='right'caption='[[1fgy]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1fgy]] is a 1 chain structure. 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> | + | <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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id=' | + | <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> | <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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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]. | </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="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. | ||
| - | |||
| - | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1fgy" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Bose | + | [[Category: Mus musculus]] |
| - | [[Category: Chawla | + | [[Category: Bose S]] |
| - | [[Category: Cronin | + | [[Category: Chawla A]] |
| - | [[Category: Czech | + | [[Category: Cronin T]] |
| - | [[Category: Klarlund | + | [[Category: Czech MP]] |
| - | [[Category: Lambright | + | [[Category: Klarlund J]] |
| - | [[Category: Lietzke | + | [[Category: Lambright DG]] |
| - | + | [[Category: Lietzke SE]] | |
| - | + | ||
Current revision
GRP1 PH DOMAIN WITH INS(1,3,4,5)P4
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Categories: Large Structures | Mus musculus | Bose S | Chawla A | Cronin T | Czech MP | Klarlund J | Lambright DG | Lietzke SE
