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Guanylyl cyclase domain

Fig. 6.3 Model ofthe domain structure ofthe natriuretic peptide receptor NPR, a receptor-type guanylyl cyclase. NPR is a dimeric transmembrane receptor which spans the membrane with two transmembrane elements. The extracytosolic domain comprises the ligand binding site and contains several disulfide bridges. The cytosolic part is composed of a kinase homology domain with multiple phosphorylation sites, an ATP binding site of unknown function and the catalytic guanylyl cyclase domain. Fig. 6.3 Model ofthe domain structure ofthe natriuretic peptide receptor NPR, a receptor-type guanylyl cyclase. NPR is a dimeric transmembrane receptor which spans the membrane with two transmembrane elements. The extracytosolic domain comprises the ligand binding site and contains several disulfide bridges. The cytosolic part is composed of a kinase homology domain with multiple phosphorylation sites, an ATP binding site of unknown function and the catalytic guanylyl cyclase domain.
Soluble forms of guanylyl cyclase are activated by nitric oxide. These enzymes are homologous to the catalytic domains of the membrane-bound forms of GC. They are considered heterodimers because they appear to exist, under physiological conditions, as complexes of a and P subunits, each with Mr of 70-80 kDa. Both types of soluble GC contain three primary domains an amino-terminus heme domain responsible for binding nitric oxide (NO), a dimerization domain and a carboxy terminus catalytic domain. The aP heterodimer is required for enzyme activity [35]. This can be seen as similar to the situation for AC, which contains two catalytic entities within a single polypeptide chain (Fig. 21-5). [Pg.370]

CYCc Adenylyl/guanylyl cyclase, catalytic domain E(MF)B 1(1) 36(39) 1AB8... [Pg.196]

Laura, R.P., Dizhoor, A.M., and Hurley, J.B. (1996). The membrane guanylyl cyclase, retinal guanylyl cyclase-1, is activated through its intracellular domain. J. Biol. Chem. 271 11646-11651. [Pg.88]

Laura, R.P. and Hurley, J.B. (1998). The kinase homology domain of retinal guanylyl cyclases 1 and 2 specifies the affinity and cooperativity of interaction with guanylyl cyclase activating protein-2. Biochemistry 37 11264-11271. [Pg.88]

Simpson P. J., Nighom A. and Morton D. B. (1999) Identification of a novel guanylyl cyclase that is related to receptor guanylyl cyclases but lacks extracellular and transmembrane domains. J. Biol. Chem. 274, 4440-4446. [Pg.442]

Iyer LM, Anantharaman V, Aravind L. Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins. BMC Genom. 2003 4 5. [Pg.1266]

Weth F, Nadler W, Korsching S (1996) Nested expression domains for odorant receptors in zebrafish olfactory epithelium. Proc Natl Acad Sci USA 93 13321-13326 Yamagami S, Suzuki N (2005) Diverse forms of guanylyl cyclases in medaka fish - their genomic structure and phylogenetic relationships to those in vertebrates and invertebrates. Zoolog Sci 22 819-835... [Pg.69]


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