Crystal structure of the signaling helix coiled-coil domain of the beta1 subunit of the soluble guanylyl cyclase.

ABSTRACT:

Background

The soluble guanylyl cyclase (sGC) is a heterodimeric enzyme that, upon activation by nitric oxide, stimulates the production of the second messenger cGMP. Each sGC subunit harbor four domains three of which are used for heterodimerization: H-NOXA/H-NOBA domain, coiled-coil domain (CC), and catalytic guanylyl cyclase domain. The CC domain has previously been postulated to be part of a larger CC family termed the signaling helix (S-helix) family. Homodimers of sGC have also been observed but are not functionally active yet are likely transient awaiting their intended heterodimeric partner.

Results

To investigate the structure of the CC S-helix region, we crystallized and determined the structure of the CC domain of the sGCbeta1 subunit comprising residues 348-409.

SUBMITTER: Ma X 

PROVIDER: S-EPMC2828450 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature