The Structural Basis for the Allosteric Regulation of Ribonucleotide Reductase

被引：21
|
作者：
Ahmad, Md Faiz [1 ]
Dealwis, Chris G. [1 ,2 ]
机构：
[1] Case Western Reserve Univ, Sch Med, Dept Pharmacol, Cleveland, OH 44106 USA
[2] Case Western Reserve Univ, Ctr Prote & Bioinformat, Cleveland, OH 44106 USA
来源：
OLIGOMERIZATION IN HEALTH AND DISEASE | 2013年 / 117卷
关键词：
PEPTIDE INHIBITORS; COMPREHENSIVE MODEL; LARGE SUBUNIT; SUBSTRATE-SPECIFICITY; DIPHOSPHATE REDUCTASE; ENZYMATIC-SYNTHESIS; EFFECTOR-BINDING; DNA-SYNTHESIS; MECHANISM; 2-CHLORO-9-(2-DEOXY-2-FLUORO-BETA-D-ARABINOFURANOSYL)ADENINE;
D O I：
10.1016/B978-0-12-386931-9.00014-3
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：
Ribonucleotide reductases (RRs) catalyze a crucial step of de nova DNA synthesis by converting ribonucleoside diphosphates to deoxyribonucleoside diphosphates. Tight control of the dNTP pool is essential for cellular homeostasis. The activity of the enzyme is tightly regulated at the S-phase by allosteric regulation. Recent structural studies by our group and others provided the molecular basis for understanding how RR recognizes substrates, how it interacts with chemotherapeutic agents, and how it is regulated by its allosteric regulators ATP and dATP. This review discusses the molecular basis of allosteric regulation and substrate recognition of RR, and particularly the discovery that subunit oligomerization is an important prerequisite step in enzyme inhibition.
引用
收藏
页码：389 / 410
页数：22
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