or 
Receptor Family
Guanylyl Cyclase receptors
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Summary

In humans, the guanylyl cyclase receptor family includes the three known natriuretic peptide receptors (NPRs A, B, C) (48) and residues in their intracellular guanylyl cyclase domain show similarity to adenyl cyclases(49). Unliganded NPRs homo-oligomerize through several extra- and intracellular domains (50) and each receptor dimer binds one ligand molecule (51). Thus, activity is not controlled by ligand-induced dimerization but rather through conformational changes associated with ligand binding. NPR-A and NPR-B are enzymatically active. NPR-C is presumed to be a decoy receptor because it lacks the typical cytoplasmic domain (48). Membrane guanylyl cyclases have been found in nematode as well as sea urchin (52).
Relevant reviews and publications:
48. L. R. Potter, T. Hunter, Guanylyl cyclase-linked natriuretic peptide receptors: structure and regulation. J Biol Chem 276, 6057-6060 (2001). 49. C. L. Tucker, J. H. Hurley, T. R. Miller, J. B. Hurley, Two amino acid substitutions convert a guanylyl cyclase, RetGC-1, into an adenylyl cyclase. Proc Natl Acad Sci U S A 95, 5993-5997 (1998). 50. E. M. Wilson, M. Chinkers, Identification of sequences mediating guanylyl cyclase dimerization. Biochemistry 34, 4696-4701 (1995). 51. X. He, D. Chow, M. M. Martick, K. Christopher Garcia, Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone. Science 293, 1657-1662 (2001). 52. S. Singh, D. G. Lowe, D. S. Thorpe, H. Rodriguez, W. J. Kuang, L. J. Dangott, M. Chinkers, D. V. Goeddel, D. L. Garbers, Membrane guanylate cyclase is a cell-surface receptor with homology to protein kinases. Nature 334, 708-712 (1988).
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