Title : Structural insight into the substrate specificity of phosphodiesterases.

Pub. Date : 2011

PMID : 21695637






5 Functional Relationships(s)
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1 Cyclic nucleotide phosphodiesterases (PDEs) share a highly conserved catalytic domain that hydrolyzes cAMP, cGMP, or both nucleotides. Cyclic AMP phosphodiesterase 10A Homo sapiens
2 In addition, the structures of PDE10A in complex with cAMP and cGMP reveal that cAMP and cGMP bind to the active site in different orientations and have different interactions with PDE10A residues. Cyclic AMP phosphodiesterase 10A Homo sapiens
3 In addition, the structures of PDE10A in complex with cAMP and cGMP reveal that cAMP and cGMP bind to the active site in different orientations and have different interactions with PDE10A residues. Cyclic AMP phosphodiesterase 10A Homo sapiens
4 In addition, the structures of PDE10A in complex with cAMP and cGMP reveal that cAMP and cGMP bind to the active site in different orientations and have different interactions with PDE10A residues. Cyclic AMP phosphodiesterase 10A Homo sapiens
5 In addition, the structures of PDE10A in complex with cAMP and cGMP reveal that cAMP and cGMP bind to the active site in different orientations and have different interactions with PDE10A residues. Cyclic AMP phosphodiesterase 10A Homo sapiens