Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The molecular basis for different recognition of substrates by phosphodiesterase families 4 and 10.

Journal of molecular biology - 10 Aug 2007

Wang Huanchen, Robinson Howard, Ke Hengming

Abstract excerpt

Phosphodiesterases (PDEs) are key enzymes that control the cellular concentrations of the second messengers cAMP and cGMP. The mechanism for selective recognition of substrates cAMP and cGMP by individual PDE families remains a puzzle. To understand the mechanism for substrate recognition by PDE enzymes, the crystal structure of the catalytic domain of an inactive D201N mutant of PDE4D2 in complex with substrate...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Aspartic Acid
Share to Catalytic Domain
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cyclic AMP

Share to Isoenzymes

Share to Phosphoric Diester Hydrolases

Share to Protein Structure, Tertiary

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 17582435
DOI: 10.1016/j.jmb.2007.05.060
PMCID: PMC2001251

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The molecular basis for different recognition of substrates by phosphodiesterase families 4 and 10.PMID 17582435Read ↗

Structural insight into substrate specificity of phosphodiesterase 10.Semantic proximity Read ↗

Biochemistry and Physiology of Cyclic Nucleotide Phosphodiesterases: Essential Components in Cyclic Nucleotide SignalingSemantic proximity Read ↗

Overview of PDEs and their regulation.Semantic proximity Read ↗

Structural asymmetry of phosphodiesterase-9, potential protonation of a glutamic acid, and role of the invariant glutamine.Semantic proximity Read ↗

Cloning and characterization of two splice variants of human phosphodiesterase 11ASemantic proximity Read ↗

Kinetic and structural studies of phosphodiesterase-8A and implication on the inhibitor selectivity.Semantic proximity Read ↗

Cyclic AMP-specific PDE4 phosphodiesterases as critical components of cyclic AMP signaling.Semantic proximity Read ↗

Structural basis for the catalytic mechanism of human phosphodiesterase 9.Semantic proximity Read ↗

Phosphodiesterase4D (PDE4D)--A risk factor for atrial fibrillation and stroke?Semantic proximity Read ↗

The human phosphodiesterase PDE10A geneSemantic proximity Read ↗

Crystal structures of a bacterial dipeptidyl peptidase IV reveal a novel substrate recognition mechanism distinct from that of mammalian orthologues.Semantic proximity Read ↗

Insight into binding of phosphodiesterase-9A selective inhibitors by crystal structures and mutagenesis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.