1mk3

<StructureSection load='1mk3' size='340' side='right'caption='[[1mk3]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1mk3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MK3 FirstGlance]. <br>

</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=1mk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mk3 OCA], [https://pdbe.org/1mk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mk3 RCSB], [https://www.ebi.ac.uk/pdbsum/1mk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mk3 ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/B2CL2_HUMAN B2CL2_HUMAN]] Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX.<ref>PMID:8761287</ref>

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== Publication Abstract from PubMed ==

The structure of human BCL-w, an anti-apoptotic member of the BCL-2 family, was determined by triple-resonance NMR spectroscopy and molecular modeling. Introduction of a single amino acid substitution (P117V) significantly improved the quality of the NMR spectra obtained. The cytosolic domain of BCL-w consists of 8 alpha-helices, which adopt a fold similar to that of BCL-xL, BCL-2, and BAX proteins. Pairwise root meant square deviation values were less than 3 A for backbone atoms of structurally equivalent regions. Interestingly, the C-terminal helix alpha8 of BCL-w folds into the BH3-binding hydrophobic cleft of the protein, in a fashion similar to the C-terminal transmembrane helix of BAX. A peptide corresponding to the BH3 region of the pro-apoptotic protein, BID, could displace helix alpha8 from the BCL-w cleft, resulting in helix unfolding. Deletion of helix alpha8 increased binding affinities of BCL-w for BAK and BID BH3-peptides, indicating that this helix competes for peptide binding to the hydrophobic cleft. These results suggest that although the cytosolic domain of BCL-w exhibits an overall structure similar to that of BCL-xL and BCL-2, the unique organization of its C-terminal helix may modulate BCL-w interactions with pro-apoptotic binding partners.

Solution structure of human BCL-w: modulation of ligand binding by the C-terminal helix.,Denisov AY, Madiraju MS, Chen G, Khadir A, Beauparlant P, Attardo G, Shore GC, Gehring K J Biol Chem. 2003 Jun 6;278(23):21124-8. Epub 2003 Mar 21. PMID:12651847<ref>PMID:12651847</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1mk3" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Attardo, G]]

[[Category: Beauparlant, P]]

[[Category: Chen, G]]

[[Category: Denisov, A Y]]

[[Category: Gehring, K]]

[[Category: Khadir, A]]

[[Category: Madiraju, M S]]

[[Category: Shore, G C]]

[[Category: Bcl-w protein]]