1fgy

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(Difference between revisions)

Revision as of 10:42, 13 September 2017

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

Structural highlights

1fgy is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	1fgz
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CYH3_MOUSE] Promotes guanine-nucleotide exchange on ARF1. Promotes the activation of ARF factors through replacement of GDP with GTP.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ DiNitto JP, Delprato A, Gabe Lee MT, Cronin TC, Huang S, Guilherme A, Czech MP, Lambright DG. Structural basis and mechanism of autoregulation in 3-phosphoinositide-dependent Grp1 family Arf GTPase exchange factors. Mol Cell. 2007 Nov 30;28(4):569-83. PMID:18042453 doi:10.1016/j.molcel.2007.09.017
↑ Lietzke SE, Bose S, Cronin T, Klarlund J, Chawla A, Czech MP, Lambright DG. Structural basis of 3-phosphoinositide recognition by pleckstrin homology domains. Mol Cell. 2000 Aug;6(2):385-94. PMID:10983985

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==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 [http://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=1FGY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FGY FirstGlance]. <br>
+<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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FGY FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4IP:INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE'>4IP</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">[[1fgz|1fgz]]</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=1fgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgy OCA], [http://pdbe.org/1fgy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fgy RCSB], [http://www.ebi.ac.uk/pdbsum/1fgy PDBsum]</span></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=1fgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgy OCA], [http://pdbe.org/1fgy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fgy RCSB], [http://www.ebi.ac.uk/pdbsum/1fgy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fgy ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <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/chain_selection.php?pdb_ID=2ata 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="background-color:#fffaf0;">
@@ Line 33: / Line 34: @@
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
 [[Category: Bose, S]]
 [[Category: Chawla, A]]

1fgy

From Proteopedia

Revision as of 10:42, 13 September 2017

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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