Structural Perspectives on the Mechanism of Soluble Guanylate Cyclase Activation

被引：25

作者：

Wittenborn, Elizabeth C. ^{[1
,2
]}

Marletta, Michael A. ^{[1
]}

机构：

[1] Univ Calif Berkeley, Calif Inst Quantitat Biosci, Dept Chem, Berkeley, CA 94720 USA

[2] Univ Calif Berkeley, Calif Inst Quantitat Biosci, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

来源：

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | 2021年 / 22卷 / 11期

基金：

美国国家卫生研究院;

关键词：

nitric oxide; soluble guanylate cyclase; cryo-electron microscopy; enzyme structure; X-RAY-SCATTERING; NITRIC-OXIDE; CRYSTAL-STRUCTURE; CATALYTIC DOMAINS; ADENYLYL-CYCLASE; BOVINE LUNG; HEME; YC-1; EXPRESSION; SUBUNIT;

D O I：

10.3390/ijms22115439

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 enzyme soluble guanylate cyclase (sGC) is the prototypical nitric oxide (NO) receptor in humans and other higher eukaryotes and is responsible for transducing the initial NO signal to the secondary messenger cyclic guanosine monophosphate (cGMP). Generation of cGMP in turn leads to diverse physiological effects in the cardiopulmonary, vascular, and neurological systems. Given these important downstream effects, sGC has been biochemically characterized in great detail in the four decades since its discovery. Structures of full-length sGC, however, have proven elusive until very recently. In 2019, advances in single particle cryo-electron microscopy (cryo-EM) enabled visualization of full-length sGC for the first time. This review will summarize insights revealed by the structures of sGC in the unactivated and activated states and discuss their implications in the mechanism of sGC activation.

引用

页数：18

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