 |
PDBsum entry 5fe2
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Signaling protein
|
PDB id
|
|
|
|
5fe2
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structure-Based identification of inhibitory fragments targeting the p300/cbp-Associated factor bromodomain.
|
|
|
Authors
|
|
A.Chaikuad,
S.Lang,
P.E.Brennan,
C.Temperini,
O.Fedorov,
J.Hollander,
R.Nachane,
C.Abell,
S.Müller,
G.Siegal,
S.Knapp.
|
|
|
Ref.
|
|
J Med Chem, 2016,
59,
1648-1653.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
The P300/CBP-associated factor plays a central role in retroviral infection and
cancer development, and the C-terminal bromodomain provides an opportunity for
selective targeting. Here, we report several new classes of acetyl-lysine
mimetic ligands ranging from mM to low micromolar affinity that were identified
using fragment screening approaches. The binding modes of the most attractive
fragments were determined using high resolution crystal structures providing
chemical starting points and structural models for the development of potent and
selective PCAF inhibitors.
|
|
|
|
|
|
|
