An oxyanion-hole selective serine protease inhibitor in complex with trypsin

被引：12

作者：

Cui, J

Marankan, F

Fu, WT

Crich, D

Mesecar, A

Johnson, ME

机构：

[1] Univ Illinois, Coll Pharm, Ctr Pharmaceut Biotechnol, Chicago, IL 60607 USA

[2] Univ Illinois, Dept Chem, Chicago, IL 60607 USA

来源：

BIOORGANIC & MEDICINAL CHEMISTRY | 2002年 / 10卷 / 01期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/S0968-0896(01)00259-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

p-amidinophenylmethylphosphinic acid (AMPA) was designed, synthesized and crystallized in complex with trypsin to study interactions with the oxyanion hole at the S1 site. In comparison to benzamidine, AMPA shows improved activity, which the crystal structure demonstrates to result from hydrogen bonds between the negatively charged phosphinic acid group and the catalytic residues at the oxyanion hole. (C) 2001 Elsevier Science Ltd. All rights reserved.

引用

页码：41 / 46

页数：6

共 33 条

[1]

Allen F.H., 1993, CHEM AUTOMAT NEWS, V8, P31

[2]

ALLEN FH, 2000, T AM CRYSTALLOGR ASS, V32, P1

[3]

THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].