 |
PDBsum entry 3ldp
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
Adenosine-Derived inhibitors of 78 kda glucose regulated protein (grp78) atpase: insights into isoform selectivity.
|
|
|
Authors
|
|
A.T.Macias,
D.S.Williamson,
N.Allen,
J.Borgognoni,
A.Clay,
Z.Daniels,
P.Dokurno,
M.J.Drysdale,
G.L.Francis,
C.J.Graham,
R.Howes,
N.Matassova,
J.B.Murray,
R.Parsons,
T.Shaw,
A.E.Surgenor,
L.Terry,
Y.Wang,
M.Wood,
A.J.Massey.
|
|
|
Ref.
|
|
J Med Chem, 2011,
54,
4034-4041.
|
|
|
PubMed id
|
|
|
|
|
Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
|
|
|
|
Abstract
|
|
|
78 kDa glucose-regulated protein (Grp78) is a heat shock protein (HSP) involved
in protein folding that plays a role in cancer cell proliferation. Binding of
adenosine-derived inhibitors to Grp78 was characterized by surface plasmon
resonance and isothermal titration calorimetry. The most potent compounds were
13 (VER-155008) with K(D) = 80 nM and 14 with K(D) = 60 nM. X-ray crystal
structures of Grp78 bound to ATP, ADPnP, and adenosine derivative 10 revealed
differences in the binding site between Grp78 and homologous proteins.
|
|
|
|
|
|
|
