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3ihe
From Proteopedia
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| - | {{STRUCTURE_3ihe| PDB=3ihe | SCENE= }} | ||
| - | ===Crystal structure of mouse Bcl-xl mutant (F105A) at pH 6.0=== | ||
| - | {{ABSTRACT_PUBMED_20206602}} | ||
| - | == | + | ==Crystal structure of mouse Bcl-xl mutant (F105A) at pH 6.0== |
| - | [[http://www.uniprot.org/uniprot/B2CL1_MOUSE B2CL1_MOUSE | + | <StructureSection load='3ihe' size='340' side='right'caption='[[3ihe]], [[Resolution|resolution]] 3.00Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3ihe]] 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=3IHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IHE FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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=3ihe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ihe OCA], [https://pdbe.org/3ihe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ihe RCSB], [https://www.ebi.ac.uk/pdbsum/3ihe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ihe ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/B2CL1_MOUSE B2CL1_MOUSE] Potent inhibitor of cell death. Inhibits activation of caspases (By similarity). Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis.<ref>PMID:9390687</ref> Isoform Bcl-X(S) promotes apoptosis (By similarity).<ref>PMID:9390687</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/ih/3ihe_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=3ihe ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | This study reports the crystal structures of Bcl-xl wild type and three Bcl-xl mutants (Y101A, F105A, and R139A) with amino acid substitutions in the hydrophobic groove of the Bcl-xl BH3 domain. An additional 12 ordered residues were observed in a highly flexible loop between the alpha1 and alpha2 helices, and were recognized as an important deamidation site for the regulation of apoptosis. The autophagy-effector protein, Beclin 1, contains a novel BH3 domain (residues 101-125), which binds to the surface cleft of Bcl-xl, as confirmed by nuclear magnetic resonance (NMR) spectroscopy and analytical gel-filtration results. Gossypol, a potent inhibitor of Bcl-xl, had a K(d) value of 0.9 microM. In addition, the structural and biochemical analysis of five Bcl-xl substitution mutants will provide structural insights into the design and development of anti-cancer drugs. | ||
| - | + | Structural insights into mouse anti-apoptotic Bcl-xl reveal affinity for Beclin 1 and gossypol.,Priyadarshi A, Roy A, Kim KS, Kim EE, Hwang KY Biochem Biophys Res Commun. 2010 Apr 9;394(3):515-21. Epub 2010 Mar 4. PMID:20206602<ref>PMID:20206602</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | <div class="pdbe-citations 3ihe" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]] | |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Mus musculus]] | |
| - | + | [[Category: Hwang KY]] | |
| - | + | [[Category: Priyadarshi A]] | |
| - | + | ||
Current revision
Crystal structure of mouse Bcl-xl mutant (F105A) at pH 6.0
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