Structure/function of the soluble guanylyl cyclase catalytic domain

被引:26
作者
Childers, Kenneth C. [1 ]
Garcin, Elsa D. [1 ]
机构
[1] Univ Maryland Baltimore Cty, Dept Chem & Biochem, 1000 Hilltop Circle, Baltimore, MD 21250 USA
来源
NITRIC OXIDE-BIOLOGY AND CHEMISTRY | 2018年 / 77卷
基金
美国国家卫生研究院;
关键词
Soluble guanylyl cyclase; Adenylyl cyclase; Catalytic domain; Nitric oxide; S-nitrosation; Activation mechanism; NITRIC-OXIDE RECEPTOR; ADENYLYL-CYCLASE; CRYSTAL-STRUCTURE; YC-1; BINDING; FUNCTIONAL-CHARACTERIZATION; DIFFERENTIAL INHIBITION; SIGNALING HELIX; BETA-1; SUBUNIT; HEME; ACTIVATION;
D O I
10.1016/j.niox.2018.04.008
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
Soluble guanylyl cyclase (GC-1) is the primary receptor of nitric oxide (NO) in smooth muscle cells and maintains vascular function by inducing vasorelaxation in nearby blood vessels. GC-1 converts guanosine 5'-triphosphate (GTP) into cyclic guanosine 3',5'-monophosphate (cGMP), which acts as a second messenger to improve blood flow. While much work has been done to characterize this pathway, we lack a mechanistic understanding of how NO binding to the heme domain leads to a large increase in activity at the C-terminal catalytic domain. Recent structural evidence and activity measurements from multiple groups have revealed a low-activity cyclase domain that requires additional GC-1 domains to promote a catalytically-competent conformation. How the catalytic domain structurally transitions into the active conformation requires further characterization. This review focuses on structure/function studies of the GC-1 catalytic domain and recent advances various groups have made in understanding how catalytic activity is regulated including small molecules interactions, Cys-S-NO modifications and potential interactions with the NO-sensor domain and other proteins.
引用
收藏
页码:53 / 64
页数:12
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