A molecular view of the regulation of sGC activity

摘要: Mammalian sGC is a heterodimer composed of α- and β-subunits (Figure ​(Figure1).1). The C-terminus each subunit contains catalytic domain the active site residues from both subunits. domains also form pseudosymmetric that known to be involved in nucleotide binding, but lack amino acids required for catalysis. Sequence analysis shows well-defined PAS-like domain, predicted helical region. N-termini are homologous H-NOX (Heme-Nitric oxide/OXygen) family proteins. N-terminus β-subunit ferrous heme cofactor serves receptor NO. activity modulated by ATP substrate GTP recent studies point toward more complicated role NO regulation activity. Structural results coupled with biochemical cellular experiments have broadened current molecular view sGC. Figure 1 Domain structure sGC.