2jm6: Difference between revisions
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'''Solution structure of MCL-1 complexed with NOXAB''' | '''Solution structure of MCL-1 complexed with NOXAB''' | ||
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[[Category: Lee, E F.]] | [[Category: Lee, E F.]] | ||
[[Category: Smith, B J.]] | [[Category: Smith, B J.]] | ||
[[Category: | [[Category: Apoptosis]] | ||
[[Category: | [[Category: Bcl-2]] | ||
[[Category: | [[Category: Bh3-only]] | ||
[[Category: | [[Category: Helical bundle]] | ||
[[Category: | [[Category: Mcl-1]] | ||
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Revision as of 06:01, 4 May 2008
Solution structure of MCL-1 complexed with NOXAB
Overview
Apoptosis is held in check by prosurvival proteins of the Bcl-2 family. The distantly related BH3-only proteins bind to and antagonize them, thereby promoting apoptosis. Whereas binding of the BH3-only protein Noxa to prosurvival Mcl-1 induces Mcl-1 degradation by the proteasome, binding of another BH3-only ligand, Bim, elevates Mcl-1 protein levels. We compared the three-dimensional structures of the complexes formed between BH3 peptides of both Bim and Noxa, and we show that a discrete C-terminal sequence of the Noxa BH3 is necessary to instigate Mcl-1 degradation.
About this Structure
2JM6 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural insights into the degradation of Mcl-1 induced by BH3 domains., Czabotar PE, Lee EF, van Delft MF, Day CL, Smith BJ, Huang DC, Fairlie WD, Hinds MG, Colman PM, Proc Natl Acad Sci U S A. 2007 Apr 10;104(15):6217-22. Epub 2007 Mar 27. PMID:17389404 Page seeded by OCA on Sun May 4 09:01:16 2008