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PMID: 7651533 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

Nature ·Vol. 376 ·No. 6543 ·1995-08-31 ·Pages 745-53

Goldberg J, Huang HB, Kwon YG, Greengard P, Nairn AC, Kuriyan J

Abstract

The crystal structure of mammalian protein phosphatase-1, complexed with the toxin microcystin and determined at 2.1 A resolution, reveals that it is a metalloenzyme unrelated in architecture to the tyrosine phosphatases. Two metal ions are positioned by a central beta-alpha-beta-alpha-beta scaffold at the active site, from which emanate three surface grooves that are potential binding sites for substrates and inhibitors. The carboxy terminus is positioned at the end of one of the grooves such that regulatory sequences following the domain might modulate function. The fold of the catalytic domain is expected to be closely preserved in protein phosphatases 2A and 2B (calcineurin).

MeSH Terms
Amino Acid Sequence Animals Binding Sites Catalysis Crystallography, X-Ray Dopamine and cAMP-Regulated Phosphoprotein 32 Escherichia coli Humans Intracellular Signaling Peptides and Proteins Metals/chemistry Microcystins Models, Molecular Molecular Sequence Data Nerve Tissue Proteins/chemistry Nuclear Proteins Peptides, Cyclic/chemistry Phosphoprotein Phosphatases/antagonists & inhibitors,chemistry Phosphoproteins Protein Conformation Protein Phosphatase 1 Proteins/chemistry RNA-Binding Proteins Rabbits Recombinant Proteins/chemistry Sequence Homology, Amino Acid
Chemicals
ANP32A protein, human Dopamine and cAMP-Regulated Phosphoprotein 32 Intracellular Signaling Peptides and Proteins Metals Microcystins Nerve Tissue Proteins Nuclear Proteins Peptides, Cyclic Phosphoproteins Proteins RNA-Binding Proteins Recombinant Proteins microcystin Phosphoprotein Phosphatases Protein Phosphatase 1
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Goldberg J
Howard Hughes Medical Institute, Rockefeller University, New York, New York 10021, USA.
Huang H B
Kwon Y G
Greengard P
Nairn A C
Kuriyan J
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1995-08-31
Pages
745-53
Language
English
Region
England
NLM ID
0410462
Subset
IM
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