Poulos Thomas L
Department of Molecular Biology & Biochemistry, University of California Irvine, Irvine, CA 92697-3900, USA.
Curr Opin Struct Biol. 2006 Dec;16(6):736-43. doi: 10.1016/j.sbi.2006.09.006. Epub 2006 Oct 2.
Soluble guanylate cyclase (sGC) is a mammalian nitric oxide (NO) sensor. When NO binds to the sGC heme, its GTP cyclase activity markedly increases, thus generating cyclic GMP, which serves to regulate several cell signaling functions. A good deal is known about the kinetics and equilibrium of binding of NO to sGC, leading to a proposed multistep mechanism of sGC activation that involves at least two NO-binding sites. The crystal structure of a member of a recently discovered family of prokaryotic sGC homologues has provided important insights into structure-function relationships within the sGC family of proteins.
可溶性鸟苷酸环化酶（sGC）是一种哺乳动物一氧化氮（NO）传感器。当NO与sGC血红素结合时，其GTP环化酶活性显著增加，从而生成环磷酸鸟苷（cGMP），后者用于调节多种细胞信号传导功能。关于NO与sGC结合的动力学和平衡已有很多了解，由此提出了一种sGC激活的多步骤机制，该机制涉及至少两个NO结合位点。最近发现的原核sGC同源物家族中一个成员的晶体结构，为深入了解sGC蛋白家族内的结构-功能关系提供了重要线索。
