Structural comparison analysis of 2H phosphodiesterase family proteins | Zendy

Yasumitsu Sakamoto | Zendy; Nobutada Tanaka | Zendy; Tomomi Ichimiya | Zendy; T. Kurihara | Zendy; Kohei Nakamura | Zendy

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Structural comparison analysis of 2H phosphodiesterase family proteins

Author(s) -

Yasumitsu Sakamoto,

Nobutada Tanaka,

Tomomi Ichimiya,

T. Kurihara,

Kohei Nakamura

Publication year - 2007

Publication title -

nucleic acids symposium series

Language(s) - English

Resource type - Journals

eISSN - 1746-8272

pISSN - 0261-3166

DOI - 10.1093/nass/nrm224

Subject(s) - phosphodiesterase , nucleotide , cyclic nucleotide phosphodiesterase , hydrolysis , chemistry , biochemistry , nuclear magnetic resonance spectroscopy , cyclic nucleotide , in vitro , protein structure , function (biology) , stereochemistry , biology , crystallography , enzyme , microbiology and biotechnology , gene

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.

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