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== | ==SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF RGL== | ||
<StructureSection load='1ef5' size='340' side='right'caption='[[1ef5]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1ef5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EF5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1ef5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ef5 OCA], [https://pdbe.org/1ef5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ef5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ef5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ef5 ProSAT], [https://www.topsan.org/Proteins/RSGI/1ef5 TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RGL1_MOUSE RGL1_MOUSE] Probable guanine nucleotide exchange factor. | |||
== 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/ef/1ef5_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1ef5 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The RGL protein, a homolog of the Ral GDP dissociation stimulator (RalGDS), has been identified as a downstream effector of Ras. In the present study, the solution structure of the Ras-binding domain of RGL (RGL-RBD) was determined by NMR spectroscopy. The overall fold of RGL-RBD consists of a five-stranded beta-sheet and two alpha-helices, which is the same topology as that of RalGDS-RBD. The backbone chemical shift perturbation of RGL-RBD upon interaction with the GTP analog-bound Ras was also examined. The solution structure of RGL-RBD, especially around some of the Ras-interacting residues, is appreciably different from that of RalGDS-RBD. | The RGL protein, a homolog of the Ral GDP dissociation stimulator (RalGDS), has been identified as a downstream effector of Ras. In the present study, the solution structure of the Ras-binding domain of RGL (RGL-RBD) was determined by NMR spectroscopy. The overall fold of RGL-RBD consists of a five-stranded beta-sheet and two alpha-helices, which is the same topology as that of RalGDS-RBD. The backbone chemical shift perturbation of RGL-RBD upon interaction with the GTP analog-bound Ras was also examined. The solution structure of RGL-RBD, especially around some of the Ras-interacting residues, is appreciably different from that of RalGDS-RBD. | ||
Solution structure of the Ras-binding domain of RGL.,Kigawa T, Endo M, Ito Y, Shirouzu M, Kikuchi A, Yokoyama S FEBS Lett. 1998 Dec 28;441(3):413-8. PMID:9891982<ref>PMID:9891982</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1ef5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Endo M]] | |||
[[Category: Endo | [[Category: Ito Y]] | ||
[[Category: Ito | [[Category: Kigawa T]] | ||
[[Category: Kigawa | [[Category: Kikuchi A]] | ||
[[Category: Kikuchi | [[Category: Shirouzu M]] | ||
[[Category: Yokoyama S]] | |||
[[Category: Shirouzu | |||
[[Category: Yokoyama | |||
Latest revision as of 11:26, 22 May 2024
SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF RGLSOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF RGL
Structural highlights
FunctionRGL1_MOUSE Probable guanine nucleotide exchange factor. 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 PubMedThe RGL protein, a homolog of the Ral GDP dissociation stimulator (RalGDS), has been identified as a downstream effector of Ras. In the present study, the solution structure of the Ras-binding domain of RGL (RGL-RBD) was determined by NMR spectroscopy. The overall fold of RGL-RBD consists of a five-stranded beta-sheet and two alpha-helices, which is the same topology as that of RalGDS-RBD. The backbone chemical shift perturbation of RGL-RBD upon interaction with the GTP analog-bound Ras was also examined. The solution structure of RGL-RBD, especially around some of the Ras-interacting residues, is appreciably different from that of RalGDS-RBD. Solution structure of the Ras-binding domain of RGL.,Kigawa T, Endo M, Ito Y, Shirouzu M, Kikuchi A, Yokoyama S FEBS Lett. 1998 Dec 28;441(3):413-8. PMID:9891982[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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