Cofactor-binding sites in proteins of deviating sequence: Comparative analysis and clustering in torsion angle, cavity, and fold space-Reference-Cited by-同舟云学术

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Cofactor-binding sites in proteins of deviating sequence: Comparative analysis and clustering in torsion angle, cavity, and fold space

Published:2011-11-17 Issue:2 Volume:80 Page:626-648
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Stegemann Björn,Klebe Gerhard

Funder

German Government for the Rehabilitation of Disabled People

the Hermann-Leuschner Stiftung

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/prot.23226/fullpdf

Reference92 articles.

1. The importance of discerning shape in molecular pharmacology;Kortagere;Trends Pharmacol Sci,2009

2. Shape variation in protein binding pockets and their ligands;Kahraman;J Mol Biol,2007

3. Rational design of transition-state analogues as potent enzyme inhibitors with therapeutic applications;Amyes;ACS Chem Biol,2007

4. The topology of drug-target interaction networks: implicit dependence on drug properties and target families;Mestres;Mol BioSyst,2009

5. Geometry of binding of the benzamidine- and arginine-based inhibitors Nα-(2-naphthyl-sulphonyl-glycyl)-dl-p-amidinophenylalanyl-piperidine (NAPAP) and (2R,4R)-4-methyl-1-[Nα-(3-methyl-1,2,3,4-tetrahydro-8-quinolinesulphonyl)-l-arginyl]-2-piperidine carboxylic acid (MQPA) to human α-thrombin. X-ray crystallographic determination of the NAPAP-trypsin complex and modeling of NAPAP-thrombin and MQPA-thrombin;Bode;Eur J Biochem,1990

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