1g5j
From Proteopedia
(Difference between revisions)
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==COMPLEX OF BCL-XL WITH PEPTIDE FROM BAD== | ==COMPLEX OF BCL-XL WITH PEPTIDE FROM BAD== | ||
| - | <StructureSection load='1g5j' size='340' side='right'caption='[[1g5j | + | <StructureSection load='1g5j' size='340' side='right'caption='[[1g5j]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1g5j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1g5j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G5J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G5J 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">Solution NMR</td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g5j OCA], [https://pdbe.org/1g5j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g5j RCSB], [https://www.ebi.ac.uk/pdbsum/1g5j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g5j 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=1g5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g5j OCA], [https://pdbe.org/1g5j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g5j RCSB], [https://www.ebi.ac.uk/pdbsum/1g5j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g5j ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/B2CL1_HUMAN B2CL1_HUMAN] 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:19917720</ref> <ref>PMID:21840391</ref> Isoform Bcl-X(S) promotes apoptosis.<ref>PMID:19917720</ref> <ref>PMID:21840391</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=1g5j 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=1g5j ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The three-dimensional structure of the anti-apoptotic protein Bcl-xL complexed to a 25-residue peptide from the death promoting region of Bad was determined using NMR spectroscopy. Although the overall structure is similar to Bcl-xL bound to a 16-residue peptide from the Bak protein (Sattler et al., 1997), the Bad peptide forms additional interactions with Bcl-xL. However, based upon site-directed mutagenesis experiments, these additional contacts do not account for the increased affinity of the Bad 25-mer for Bcl-xL compared to the Bad 16-mer. Rather, the increased helix propensity of the Bad 25-mer is primarily responsible for its greater affinity for Bcl-xL. Based on this observation, a pair of 16-residue peptides were designed and synthesized that were predicted to have a high helix propensity while maintaining the interactions important for complexation with Bcl-xL. Both peptides showed an increase in helix propensity compared to the wild-type and exhibited an enhanced affinity for Bcl-xL. | ||
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| - | Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies.,Petros AM, Nettesheim DG, Wang Y, Olejniczak ET, Meadows RP, Mack J, Swift K, Matayoshi ED, Zhang H, Thompson CB, Fesik SW Protein Sci. 2000 Dec;9(12):2528-34. PMID:11206074<ref>PMID:11206074</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1g5j" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Fesik | + | [[Category: Fesik SW]] |
| - | [[Category: Mack | + | [[Category: Mack J]] |
| - | [[Category: Matayoshi | + | [[Category: Matayoshi ED]] |
| - | [[Category: Meadows | + | [[Category: Meadows RP]] |
| - | [[Category: Nettesheim | + | [[Category: Nettesheim DG]] |
| - | [[Category: Olejniczak | + | [[Category: Olejniczak ET]] |
| - | [[Category: Petros | + | [[Category: Petros AM]] |
| - | [[Category: Swift | + | [[Category: Swift K]] |
| - | [[Category: Thompson | + | [[Category: Thompson CB]] |
| - | [[Category: Wang | + | [[Category: Wang Y]] |
| - | [[Category: Zhang | + | [[Category: Zhang H]] |
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Revision as of 11:19, 27 March 2024
COMPLEX OF BCL-XL WITH PEPTIDE FROM BAD
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Categories: Homo sapiens | Large Structures | Fesik SW | Mack J | Matayoshi ED | Meadows RP | Nettesheim DG | Olejniczak ET | Petros AM | Swift K | Thompson CB | Wang Y | Zhang H
