3'5'-cyclic nucleotide phosphodiesterase, conserved site
IPR023174
Definition
3'5'-cyclic nucleotide phosphodiesterases ([ec:3.1.4.17]) (PDEases) catalyse the hydrolysis of cAMP or cGMP to the corresponding nucleoside 5' monophosphates PMID:3025833. There are at least seven different subfamilies of PDEases PMID:2159198: Type 1, calmodulin/calcium-dependent PDEases. Type 2, cGMP-stimulated PDEases. Type 3, cGMP-inhibited PDEases. Type 4, cAMP-specific PDEases. Type 5, cGMP-specific PDEases. Type 6, rhodopsin-sensitive cGMP-specific PDEases. Type 7, High affinity cAMP-specific PDEases. All of these forms seem to share a conserved domain of about 270 residues. This entry has a signature pattern from a stretch of 12 residues that contains two conserved histidines. The PDEase catalytic domains adopt a compact α-helical structure consisting of 16 α-helices that can be divided into three subdomains. The active site of PDEases is a deep pocket formed by the tree subdomains and can be divided into two major subpockets for binding of divalent metals and substrate/inhibitors, respectively. The active site of all PDEase domains contains two divalent metal ions: zinc and probably magnesium [[cite:PMID:15260978], [cite:PMID:10846163], [cite:PMID:17305581]].
21 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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