Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1979739 | Current Opinion in Structural Biology | 2006 | 8 Pages |
Abstract
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.
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Authors
Thomas L Poulos,