3cg6

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Current revision (09:35, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3cg6' size='340' side='right'caption='[[3cg6]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='3cg6' size='340' side='right'caption='[[3cg6]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3cg6]] is a 2 chain structure with sequence from [https://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=3CG6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CG6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3cg6]] is a 2 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=3CG6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CG6 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Gadd45g ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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=3cg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cg6 OCA], [https://pdbe.org/3cg6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cg6 RCSB], [https://www.ebi.ac.uk/pdbsum/3cg6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cg6 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=3cg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cg6 OCA], [https://pdbe.org/3cg6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cg6 RCSB], [https://www.ebi.ac.uk/pdbsum/3cg6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cg6 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GA45G_MOUSE GA45G_MOUSE] Involved in the regulation of growth and apoptosis. Mediates activation of stress-responsive MTK1/MEKK4 MAPKKK.
== 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=3cg6 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=3cg6 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Gadd45 proteins are recognized as tumor and autoimmune suppressors whose expression can be induced by genotoxic stresses. These proteins are involved in cell cycle control, growth arrest, and apoptosis through interactions with a wide variety of binding partners. We report here the crystal structure of Gadd45gamma, which reveals a fold comprising an alphabetaalpha sandwich with a central five-stranded mixed beta-sheet with alpha-helices packed on either side. Based on crystallographic symmetry we identified the dimer interface of Gadd45gamma dimers by generating point mutants that compromised dimerization while leaving the tertiary structure of the monomer intact. The dimer interface comprises a four-helix bundle involving residues that are the most highly conserved among Gadd45 isoforms. Cell-based assays using these point mutants demonstrate that dimerization is essential for growth inhibition. This structural information provides a new context for evaluation of the plethora of protein-protein interactions that govern the many functions of the Gadd45 family of proteins.
 
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The crystal structure and dimerization interface of GADD45gamma.,Schrag JD, Jiralerspong S, Banville M, Jaramillo ML, O'Connor-McCourt MD Proc Natl Acad Sci U S A. 2008 May 6;105(18):6566-71. Epub 2008 Apr 29. PMID:18445651<ref>PMID:18445651</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 3cg6" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Mus musculus]]
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[[Category: Banville, M]]
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[[Category: Banville M]]
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[[Category: Connor-McCourt, M D.O]]
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[[Category: Jaramillo ML]]
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[[Category: Jaramillo, M L]]
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[[Category: Jiralerspong S]]
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[[Category: Jiralerspong, S]]
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[[Category: O'Connor-McCourt MD]]
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[[Category: Schrag, J D]]
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[[Category: Schrag JD]]
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[[Category: Alpha/beta]]
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[[Category: Cell cycle]]
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Current revision

Crystal structure of Gadd45 gamma

PDB ID 3cg6

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