The structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for anti-malarial design

被引：141

作者：

Dunn, CR

Banfield, MJ

Barker, JJ

Higham, CW

Moreton, KM

Turgut-Balik, D

Brady, RL

Holbrook, JJ

机构：

[1] UNIV BRISTOL, SCH MED SCI, MOL RECOGNIT CTR, BRISTOL BS8 1TD, AVON, ENGLAND

[2] UNIV BRISTOL, SCH MED SCI, DEPT BIOCHEM, BRISTOL BS8 1TD, AVON, ENGLAND

来源：

NATURE STRUCTURAL BIOLOGY | 1996年 / 3卷 / 11期

关键词：

D O I：

10.1038/nsb1196-912

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The crystal structure of Plasmodium falciparum lactate dehydrogenase reveals a surprising shift in the position of the NADH cofactor that explains the unusual biochemical properties of this enzyme. There is also a distinctive surface cleft adjacent to the NADH binding pocket that forms an attractive target for inhibitor design.

引用

页码：912 / 915

页数：4

共 20 条

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