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Open Access

Structural insights into sGC

  • Focco van den Akker1Email author,
  • Xiaolei Ma2,
  • Faye Martin1,
  • Priyaranjan Pattanaik3,
  • Pius Padayatti4,
  • Matthew Warman5 and
  • Annie Beuve6
BMC Pharmacology20099(Suppl 1):S42

https://doi.org/10.1186/1471-2210-9-S1-S42

Published: 11 August 2009

The membrane and soluble guanylyl cyclases (sGCs) are key families of enzymes that produce the second messenger cGMP. Although both families recognize different ligands and have therefore different N-terminal input domains, they do have similar C-terminal output domains containing a coiled-coil domain and a guanylyl cyclase catalytic domain. We present here our latest structure-function studies on both the sGC and membrane guanylyl cyclases in an effort to enhance our molecular understanding of these receptors to delineate their similarities and differences. Our studies include a new 2.15 Å crystal structure of part of sGC and mutagenesis studies of these families of guanylyl cyclases thereby providing new insights into the structure, activation, and regulation of these receptors.

Authors’ Affiliations

(1)
Department of Biochemistry/RT500, Case Western Reserve University
(2)
Genentech
(3)
(4)
Polgenix
(5)
Harvard Medical School
(6)
UMNDJ

Copyright

© Akker et al; licensee BioMed Central Ltd. 2009

This article is published under license to BioMed Central Ltd.

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