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Article

The role of tryptophan 1072 in human PDE3B inhibitor binding.

Biochemical and biophysical research communications - 8 Aug 2003

Chung Christine, Varnerin Jeffrey P, Morin Nancy R, MacNeil Douglas J, Singh Suresh B, Patel Sangita, Scapin Giovanna, Van der Ploeg Lex H T, Tota Michael R

Abstract excerpt

The catalytic domain of recombinant human PDE3B was expressed in Escherichia coli as inclusion bodies and refolded to form active enzyme. A mutation at tryptophan 1072 in PDE3B disrupts inhibitor binding, but has minimal effect on cAMP hydrolysis. The W1072A mutation caused a 158-fold decrease in affinity for cilostamide, a 740-fold decrease for cGMP, and a 15-fold decrease in affinity for IBMX. The corresponding...

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Identifiers

PMID: 12878217
DOI: 10.1016/s0006-291x(03)01299-3

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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