| Structural highlights
Publication Abstract from PubMed
Herein we report the discovery of a family of novel yet simple, amino-acid derived class I HDAC inhibitors that demonstrate isoform selectivity via access to the internal acetate release channel. Isoform selectivity criteria is discussed on the basis of X-ray crystallography and molecular modeling of these novel inhibitors bound to HDAC8, potentially revealing insights into the mechanism of enzymatic function through novel structural features revealed at the atomic level.
Human HDAC isoform selectivity achieved via exploitation of the acetate release channel with structurally unique small molecule inhibitors.,Whitehead L, Dobler MR, Radetich B, Zhu Y, Atadja PW, Claiborne T, Grob JE, McRiner A, Pancost MR, Patnaik A, Shao W, Shultz M, Tichkule R, Tommasi RA, Vash B, Wang P, Stams T Bioorg Med Chem. 2011 Aug 1;19(15):4626-34. Epub 2011 Jun 15. PMID:21723733[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Whitehead L, Dobler MR, Radetich B, Zhu Y, Atadja PW, Claiborne T, Grob JE, McRiner A, Pancost MR, Patnaik A, Shao W, Shultz M, Tichkule R, Tommasi RA, Vash B, Wang P, Stams T. Human HDAC isoform selectivity achieved via exploitation of the acetate release channel with structurally unique small molecule inhibitors. Bioorg Med Chem. 2011 Aug 1;19(15):4626-34. Epub 2011 Jun 15. PMID:21723733 doi:10.1016/j.bmc.2011.06.030
|
