Different orientations of low-molecular-weight fragments in the binding pocket of a BRD4 bromodomain
2013 ◽
Vol 69
(10)
◽
pp. 2161-2164
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Keyword(s):
Bromodomains are involved in the regulation of chromatin architecture and transcription through the recognition of acetylated lysines in histones and other proteins. Many of them are considered to be relevant pharmacological targets for different pathologies. Three crystallographic structures of the N-terminal bromodomain of BRD4 in complex with low-molecular-weight fragments are presented. They show that similar molecules mimicking acetylated lysine bind the bromodomain with different orientations and exploit different interactions. It is also advised to avoid DMSO when searching for low-affinity fragments that interact with bromodomains since DMSO binds in the acetylated lysine-recognition pocket of BRD4.
1978 ◽
Vol 36
(1)
◽
pp. 110-111
1998 ◽
Vol 1
(5)
◽
pp. 166-174
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2004 ◽
Vol 3
(1)
◽
pp. 118
1986 ◽
Vol 131
(3)
◽
pp. 361-385