2me8
From Proteopedia
(Difference between revisions)
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<StructureSection load='2me8' size='340' side='right' caption='[[2me8]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2me8' size='340' side='right' caption='[[2me8]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2me8]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ME8 OCA]. <br> | + | <table><tr><td colspan='2'>[[2me8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ME8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ME8 FirstGlance]. <br> |
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2me9|2me9]], [[2mej|2mej]]</td></tr> | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2me9|2me9]], [[2mej|2mej]]</td></tr> | ||
| - | <tr><td class="sblockLbl"><b> | + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BCL2L1, BCL2L, BCLX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
<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=2me8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2me8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2me8 RCSB], [http://www.ebi.ac.uk/pdbsum/2me8 PDBsum]</span></td></tr> | <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=2me8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2me8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2me8 RCSB], [http://www.ebi.ac.uk/pdbsum/2me8 PDBsum]</span></td></tr> | ||
<table> | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Follis, A Viacava.]] | [[Category: Follis, A Viacava.]] | ||
[[Category: Grace, C R.]] | [[Category: Grace, C R.]] | ||
Revision as of 06:11, 9 July 2014
Solution Structure of BCL-xL in its p53-bound conformation determined with selective isotope labelling of I,L,V sidechains
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