2. Academic Validation
  3. Adenosine-derived inhibitors of 78 kDa glucose regulated protein (Grp78) ATPase: insights into isoform selectivity

Adenosine-derived inhibitors of 78 kDa glucose regulated protein (Grp78) ATPase: insights into isoform selectivity

  • J Med Chem. 2011 Jun 23;54(12):4034-41. doi: 10.1021/jm101625x.
Alba T Macias 1,  Douglas S Williamson,  Nicola Allen,  Jenifer Borgognoni,  Alexandra Clay,  Zoe Daniels,  Pawel Dokurno,  Martin J Drysdale,  Geraint L Francis,  Christopher J Graham,  Rob Howes,  Natalia Matassova,  James B Murray,  Rachel Parsons,  Terry Shaw,  Allan E Surgenor,  Lindsey Terry,  Yikang Wang,  Mike Wood,  Andrew J Massey
Affiliations

Affiliation

  • 1 Vernalis (R&D) Ltd., Granta Park, Great Abington, Cambridge, CB21 6GB, UK. a.macias@vernalis.com
PMID: 21526763 DOI: 10.1021/jm101625x
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.

Figures
嗨！很高兴为您提供帮助！

尊敬的 MCE 客户您好，
请您选择所在区域，我们将转接对应客服为您服务！

热门区域

A

B

C

F

G

H

J

L

N

Q

S

T

X

Y

Z

热 A B C F G H J L N Q S T X Y Z