Ontology highlight
ABSTRACT:
SUBMITTER: Wang H
PROVIDER: S-EPMC1851569 | biostudies-literature | 2007 Apr
REPOSITORIES: biostudies-literature
Wang Huanchen H Liu Yudong Y Hou Jing J Zheng Meiyan M Robinson Howard H Ke Hengming H
Proceedings of the National Academy of Sciences of the United States of America 20070326 14
Phosphodiesterases (PDEs) hydrolyze the second messengers cAMP and cGMP. It remains unknown how individual PDE families selectively recognize cAMP and cGMP. This work reports structural studies on substrate specificity. The crystal structures of the catalytic domains of the D674A and D564N mutants of PDE10A2 in complex with cAMP and cGMP reveal that two substrates bind to the active site with the same syn configuration but different orientations and interactions. The products AMP and GMP bind PD ...[more]