Title : Three-dimensional structures of PDE4D in complex with roliprams and implication on inhibitor selectivity.

Pub. Date : 2003 Jul

PMID : 12842049






5 Functional Relationships(s)
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1 The corresponding Y329S mutation in PDE7 may lead to loss of the hydrogen bonds between rolipram and Gln369 and is thus a possible reason explaining PDE7"s insensitivity to rolipram inhibition. Hydrogen phosphodiesterase 7A Homo sapiens
2 The corresponding Y329S mutation in PDE7 may lead to loss of the hydrogen bonds between rolipram and Gln369 and is thus a possible reason explaining PDE7"s insensitivity to rolipram inhibition. Hydrogen phosphodiesterase 7A Homo sapiens
3 The corresponding Y329S mutation in PDE7 may lead to loss of the hydrogen bonds between rolipram and Gln369 and is thus a possible reason explaining PDE7"s insensitivity to rolipram inhibition. Rolipram phosphodiesterase 7A Homo sapiens
4 The corresponding Y329S mutation in PDE7 may lead to loss of the hydrogen bonds between rolipram and Gln369 and is thus a possible reason explaining PDE7"s insensitivity to rolipram inhibition. Rolipram phosphodiesterase 7A Homo sapiens
5 The corresponding Y329S mutation in PDE7 may lead to loss of the hydrogen bonds between rolipram and Gln369 and is thus a possible reason explaining PDE7"s insensitivity to rolipram inhibition. Rolipram phosphodiesterase 7A Homo sapiens