The linker region in receptor guanylyl cyclases is a key regulatory module: mutational analysis of guanylyl cyclase C.

ABSTRACT: Receptor guanylyl cyclases are multidomain proteins, and ligand binding to the extracellular domain increases the levels of intracellular cGMP. The intracellular domain of these receptors is composed of a kinase homology domain (KHD), a linker of approximately 70 amino acids, followed by the C-terminal guanylyl cyclase domain. Mechanisms by which these receptors are allosterically regulated by ligand binding to the extracellular domain and ATP binding to the KHD are not completely understood. Here we examine the role of the linker region in receptor guanylyl cyclases by a series of point mutations in receptor guanylyl cyclase C. The linker region is predicted to adopt a coiled coil structure and aid in dimerization, but we find that the effects of mutations neither follow a pattern predict

SUBMITTER: Saha S 

PROVIDER: S-EPMC2786029 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature