Crystal structure of the complex between calyculin A and the catalytic subunit of protein phosphatase 1 (Q27639005)

1

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Shigeki Matsunaga

2

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Akira Takai

3

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Hirotaka Kataiwa

4

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Toshiyuki Wakimoto

5

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Nobuhiro Fusetani

6

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Minoru Isobe

The structure and regulation of protein phosphatases

7

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publication date

May 2002

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published in

Structure

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volume

10

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issue

5

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page(s)

715-24

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cites work

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Smooth muscle myosin phosphatase inhibition and force enhancement by black sponge toxin

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Calyculin A and okadaic acid: inhibitors of protein phosphatase activity

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Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants

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Cantharidin-binding protein: identification as protein phosphatase 2A

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Insight into binding of calyculin A to protein phosphatase 1: isolation of hemicalyculin a and chemical transformation of calyculin A

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Tyrosine-272 is involved in the inhibition of protein phosphatase-1 by multiple toxins

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Site-directed mutagenesis of amino acid residues of protein phosphatase 1 involved in catalysis and inhibitor binding

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Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1

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A molecular basis for different interactions of marine toxins with protein phosphatase-1. Molecular models for bound motuporin, microcystins, okadaic acid, and calyculin A

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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.

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The solution structures of calyculin A and dephosphonocalyculin A by NMR

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Inhibition of protein phosphatase-1 by clavosines A and B. Novel members of the calyculin family of toxins

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A study of the binding requirements of calyculin A and dephosphonocalyculin A with PP1, development of a molecular recognition model for the binding interactions of the okadaic acid class of compounds with PP1.

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7 January 2021

Bioactive marine metabolites. Part 16. Calyculin A. A novel antitumor metabolite from the marine sponge Discodermia calyx

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Inhibition of specific binding of okadaic acid to protein phosphatase 2A by microcystin-LR, calyculin-A and tautomycin: method of analysis of interactions of tight-binding ligands with target protein

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Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate

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Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1

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Importance of the β12-β13 Loop in Protein Phosphatase-1 Catalytic Subunit for Inhibition by Toxins and Mammalian Protein Inhibitors

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Inhibitor-2 functions like a chaperone to fold three expressed isoforms of mammalian protein phosphatase-1 into a conformation with the specificity and regulatory properties of the native enzyme.

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Isolation of Four New Calyculins from the Marine Sponge Discodermia calyx(1)

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Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics

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Effects of a protein phosphatase inhibitor, okadaic acid, on membrane currents of isolated guinea-pig cardiac myocytes

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Apparent "activation" of protein kinases by okadaic acid class tumor promoters

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Okadaic acid: an additional non-phorbol-12-tetradecanoate-13-acetate-type tumor promoter

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Specific binding of okadaic acid, a new tumor promoter in mouse skin

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Inhibition of protein phosphatases by microcystins and nodularin associated with hepatotoxicity

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Inhibitory effect of okadaic acid on the p-nitrophenyl phosphate phosphatase activity of protein phosphatases

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Use of non-crystallographic symmetry in protein structure refinement

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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

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Effects of modification of the hydrophobic C-1-C-16 segment of tautomycin on its affinity to type-1 and type-2A protein phosphatases

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Inhibitory effect of okadaic acid derivatives on protein phosphatases. A study on structure-affinity relationship

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Estimation of the rate constants associated with the inhibitory effect of okadaic acid on type 2A protein phosphatase by time-course analysis

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Identifiers

DOI

0 references

Fatcat ID

release_ggqdxv7qhrdmhkkbbopd7w3odu

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/ggqdxv7qhrdmhkkbbopd7w3odu

24 November 2022