title: Structural comparison analysis of 2H phosphodiesterase family proteins.
abstract: 2',3'-Cyclic-nucleotide 3'-phosphodiesterase (CNP) is found mainly in the central nervous system of vertebrates and catalyzes the hydrolysis of 2',3'-cyclic nucleotides to produce 2'-nucleotides in vitro. Recently, Several 2H phosphodiesterase super family protein structures have been determined by X-ray crystallography and NMR spectroscopy. Here we report the structure-function relationship studies of two hydrophobic residues in CNP family proteins.
authors.affiliation: School of Pharmaceutical Sciences, Showa University, Tokyo 142-8555, Japan. y.sakamoto@nr.showa-u.ac.jp
authors.forename: Yasumitsu
authors.initials: Y
authors.lastname: Sakamoto
authors.forename: Nobutada
authors.initials: N
authors.lastname: Tanaka
authors.forename: Tomomi
authors.initials: T
authors.lastname: Ichimiya
authors.forename: Tadashi
authors.initials: T
authors.lastname: Kurihara
authors.forename: Kazuo T
authors.initials: KT
authors.lastname: Nakamura
mesh_terms: D063309:2',3'-Cyclic Nucleotide 3'-Phosphodiesterase; D006639:Histidine / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D010727:Phosphoric Diester Hydrolases / Q000737:chemistry* / Q000145:classification / Q000378:metabolism; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D006639:Histidine; D010727:Phosphoric Diester Hydrolases; D063309:2',3'-Cyclic Nucleotide 3'-Phosphodiesterase