2me9

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==Solution structure of BCL-xL containing the alpha1-alpha2 disordered loop determined with selective isotope labelling of I,L,V sidechains==
==Solution structure of BCL-xL containing the alpha1-alpha2 disordered loop determined with selective isotope labelling of I,L,V sidechains==
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<StructureSection load='2me9' size='340' side='right' caption='[[2me9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2me9' size='340' side='right'caption='[[2me9]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2me9]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ME9 OCA]. <br>
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<table><tr><td colspan='2'>[[2me9]] is a 1 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=2ME9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ME9 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2me8|2me8]], [[2mej|2mej]]</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">Solution NMR</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></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=2me9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2me9 OCA], [https://pdbe.org/2me9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2me9 RCSB], [https://www.ebi.ac.uk/pdbsum/2me9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2me9 ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2me9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2me9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2me9 RCSB], [http://www.ebi.ac.uk/pdbsum/2me9 PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Under conditions of genotoxic stress, human p53 activates the apoptotic effectors BAX or BAK to result in mitochondrial outer-membrane permeabilization and apoptosis. Antiapoptotic BCL-2 family member BCL-xL opposes this activity by sequestering cytosolic p53 via association with its DNA-binding domain, an interaction enhanced by p53 tetramerization. Here we characterized the BCL-xL-p53 complex by NMR spectroscopy and modulated it through mutagenesis to determine the relative contributions of BCL-xL's interactions with p53 or other BCL-2 family proteins to the BCL-xL-dependent inhibition of UV irradiation-induced apoptosis. Under our experimental conditions, one-third of the antiapoptotic activity of BCL-xL was mediated by p53 sequestration and the remaining two-thirds through sequestration of proapoptotic BCL-2 family members. Our studies define the contributions of cytosolic p53 to UV irradiation-induced apoptosis and provide opportunities to explore its contributions to other p53-dependent apoptotic signaling pathways.
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The DNA-binding domain mediates both nuclear and cytosolic functions of p53.,Follis AV, Llambi F, Ou L, Baran K, Green DR, Kriwacki RW Nat Struct Mol Biol. 2014 Jun;21(6):535-43. doi: 10.1038/nsmb.2829. Epub 2014 May, 11. PMID:24814347<ref>PMID:24814347</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 2me9" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Follis, A Viacava.]]
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[[Category: Homo sapiens]]
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[[Category: Grace, C R.]]
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[[Category: Large Structures]]
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[[Category: Kriwacki, R W.]]
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[[Category: Grace CR]]
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[[Category: Apoptosis]]
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[[Category: Kriwacki RW]]
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[[Category: Bcl-2 family]]
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[[Category: Viacava Follis A]]
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[[Category: Bcl-xl]]
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[[Category: Cytoplasmic p53]]
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[[Category: P53]]
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[[Category: Selective labeling]]
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Current revision

Solution structure of BCL-xL containing the alpha1-alpha2 disordered loop determined with selective isotope labelling of I,L,V sidechains

PDB ID 2me9

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