2. Academic Validation
  3. Discovery of an allosteric mechanism for the regulation of HCV NS3 protein function

Discovery of an allosteric mechanism for the regulation of HCV NS3 protein function

  • Nat Chem Biol. 2012 Nov;8(11):920-5. doi: 10.1038/nchembio.1081.
Susanne M Saalau-Bethell 1,  Andrew J Woodhead,  Gianni Chessari,  Maria G Carr,  Joseph Coyle,  Brent Graham,  Steven D Hiscock,  Christopher W Murray,  Puja Pathuri,  Sharna J Rich,  Caroline J Richardson,  Pamela A Williams,  Harren Jhoti
Affiliations

Affiliation

  • 1 Astex Pharmaceuticals, Cambridge Science Park, Cambridge, UK.
PMID: 23023261 DOI: 10.1038/nchembio.1081
Abstract

Here we report a highly conserved new binding site located at the interface between the protease and helicase domains of the hepatitis C virus (HCV) NS3 protein. Using a chemical lead, identified by fragment screening and structure-guided design, we demonstrate that this site has a regulatory function on the protease activity via an allosteric mechanism. We propose that compounds binding at this allosteric site inhibit the function of the NS3 protein by stabilizing an inactive conformation and thus represent a new class of direct-acting Antiviral agents.

Figures
Products
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