A molecular modeling analysis of the binding interactions between the okadaic acid class of natural product inhibitors and the ser-thr phosphatases, PP1 and PP2A-Reference-Cited by-同舟云学术

A molecular modeling analysis of the binding interactions between the okadaic acid class of natural product inhibitors and the ser-thr phosphatases, PP1 and PP2A

Published:1997-09 Issue:9 Volume:5 Page:1751-1773
ISSN:0968-0896
Container-title:Bioorganic & Medicinal Chemistry
language:en
Short-container-title:Bioorganic & Medicinal Chemistry

Author:

Gauss Carla-Maria,Sheppeck James E.,Nairn Angus C.,Chamberlin Richard

Publisher

Elsevier BV

Subject

Organic Chemistry,Clinical Biochemistry,Drug Discovery,Pharmaceutical Science,Molecular Biology,Molecular Medicine,Biochemistry

Reference24 articles.

1. The conserved acid binding domain model of inhibitors of protein phosphatases 1 and 2A: Molecular modelling aspects.

2. An alternative computer model of the 3-dimensional structural of microcystin-LR and nodularin rationalising their interactions with protein phosphatases 1 and 2A

3. Inhibition of the ser-thr phosphatases PP1 and PP2A by naturally occurring toxins

4. Absolute configuration of tautomycin, a protein phosphatase inhibitor from a streptomycete

5. Molecular shape analysis and activity of tautomycin, a protein phosphatase inhibitor

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