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

Crystal structures of the catalytic domain of phosphodiesterase 4B complexed with AMP, 8-Br-AMP, and rolipram.

Journal of molecular biology - 19 Mar 2004

Xu Robert X, Rocque Warren J, Lambert Millard H, Vanderwall Dana E, Luther Michael A, Nolte Robert T

Abstract excerpt

Phosphodiesterase catalyzes the hydrolysis of the intracellular second messenger 3',5'-cyclic AMP (cAMP) into the corresponding 5'-nucleotide. Phosphodiesterase 4 (PDE4), the major cAMP-specific PDE in inflammatory and immune cells, is an attractive target for the treatment of asthma and COPD. We have determined crystal structures of the catalytic domain of PDE4B complexed with AMP (2.0 A), 8-Br-AMP (2.13 A) and...

Read the complete abstract on PubMed

Topics

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

Share to 3',5'-Cyclic-AMP Phosphodiesterases
Share to Adenosine Monophosphate

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Adenosine Triphosphate

Share to Cyclic Nucleotide Phosphodiesterases, Type 4

Share to In Vitro Techniques

Share to Macromolecular Substances

Share to Phosphodiesterase Inhibitors

Share to Static Electricity

Source

Identifiers

PMID: 15003452
DOI: 10.1016/j.jmb.2004.01.040

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structures of the catalytic domain of phosphodiesterase 4B complexed with AMP, 8-Br-AMP, and rolipram.PMID 15003452Read ↗

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

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

Investigating the role of N-terminal domain in phosphodiesterase 4B-inhibition by molecular dynamics simulationSemantic proximity Read ↗

Structure and regulation of the cAMP-binding domains of Epac2.Semantic proximity Read ↗

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

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

Structural and Biochemical Insight into the Mechanism of Rv2837c from Mycobacterium tuberculosis as a c-di-NMP Phosphodiesterase.Semantic proximity Read ↗

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

Molecular docking of competitive phosphodiesterase inhibitors.Semantic proximity Read ↗

Engineered stabilization and structural analysis of the autoinhibited conformation of PDE4.Semantic proximity Read ↗

Identification of inhibitor binding sites of the cAMP-specific phosphodiesterase 4.Semantic proximity Read ↗

Two-metal-Ion catalysis in adenylyl cyclase.Semantic proximity Read ↗

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