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A molecular view of the regulation of sGC activity

  • 1, 2Email author,
  • 2,
  • 1,
  • 2,
  • 1, 2,
  • 2,
  • 2 and
  • 1
BMC Pharmacology20099(Suppl 1):S27

https://doi.org/10.1186/1471-2210-9-S1-S27

Published: 11 August 2009

Keywords

  • Nucleotide
  • Sequence Analysis
  • Catalytic Domain
  • Nucleotide Binding
  • Structural Result
Mammalian sGC is a heterodimer composed of α- and β-subunits (Figure 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 (H eme-N itric oxide/OX ygen) 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
Figure 1

Domain structure of sGC.

Authors’ Affiliations

(1)
Department of Chemistry, University of California, Berkeley, USA
(2)
Department of Molecular and Cell Biology, University of California, Berkeley, USA

Copyright

© Marletta et al; licensee BioMed Central Ltd. 2009

This article is published under license to BioMed Central Ltd.

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