On the function of the internal cavity of histone deacetylase protein 8: R37 is a crucial residue for catalysis

Haider, S.M., Joseph, C.G., Neidle, S., Fierke, C.A. and Fuchter, M.J. (2011) On the function of the internal cavity of histone deacetylase protein 8: R37 is a crucial residue for catalysis. Bioorganic & Medicinal Chemistry Letters, 21 (7). pp. 2129-2132. 10.1016/j.bmcl.2011.01.128.

Full text not available from this repository.

DOI: 10.1016/j.bmcl.2011.01.128

Abstract

Biochemical studies reveal that a conserved arginine residue (R37) at the centre of the 14 Å internal cavity of histone deacetylase (HDAC) 8 is important for catalysis and acetate affinity. Computational studies indicate that R37 forms multiple hydrogen bonding interactions with the backbone carbonyl oxygen atoms of two conserved glycine residues, G303 and G305, resulting in a 'closed' form of the channel. One possible rationale for these data is that water or product (acetate) transit through the catalytically crucial internal channel of HDAC8 is regulated by a gating interaction between G139 and G303 tethered in position by the conserved R37

Item Type:Article
Uncontrolled Keywords:Acetylation; Chromatin; Epigenetic; HDAC; Histones
Departments, units and centres:Department of Pharmaceutical and Biological Chemistry > Department of Pharmaceutical and Biological Chemistry
ID Code:2735
Journal or Publication Title:Bioorganic & Medicinal Chemistry Letters
Deposited By:Library Staff
Deposited On:20 Jan 2012 11:55
Last Modified:20 Jan 2012 11:55

Repository Staff Only: Item control page

School of Pharmacy Staff Only: Edit a copy to replace this item