Year: 2009
Type: article
Abstract: Mammalian sGC is a heterodimer composed of α- and β-subunits (Figure (Figure1).1). The C-terminus of each subunit contains a catalytic domain and the active site is composed of residues from both subunits. The catalytic domains also form a pseudosymmetric active site that contains residues known to be involved in nucleotide binding, but lack the amino acids required for catalysis. Sequence analysis shows that each subunit also contains well-defined PAS-like domain, and a predicted helical region. The N-termini of the α- and β-subunits are homologous to the H-NOX (Heme-Nitric oxide/OXygen) family of proteins. The N-terminus of β-subunit contains a ferrous heme cofactor that serves a receptor for NO. sGC activity is also modulated by ATP and the substrate GTP and recent studies point toward a more complicated role for NO in the regulation of activity. Structural results coupled with biochemical and cellular experiments have broadened the current molecular view of the regulation of sGC.
Figure 1
Domain structure of sGC.
Source: BMC Pharmacology
Institution: University of California, Berkeley
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: hybrid
OpenAlex ID: W2094546319