PROTEIN PHOSPHATASES - STRUCTURE AND FUNCTION (A REVIEW)

Citation
Eg. Bulanova et Vm. Budagyan, PROTEIN PHOSPHATASES - STRUCTURE AND FUNCTION (A REVIEW), Molecular biology, 28(5), 1994, pp. 639-645
Citations number
112
Categorie Soggetti
Biology
Journal title
ISSN journal
00268933
Volume
28
Issue
5
Year of publication
1994
Part
1
Pages
639 - 645
Database
ISI
SICI code
0026-8933(1994)28:5<639:PP-SAF>2.0.ZU;2-3
Abstract
Phosphorylation of proteins and enzymes is crucial for cell growth, di fferentiation, division and mitosis. Phosphorylation causes conformati onal changes in a protein resulting in most cases in its increased enz ymic activity and in more efficient substrate binding. Phosphorylation is effected by a variety of protein kinases. These enzymes are classi fied as tyrosine and serine protein kinases in accord with the amino a cid residues to be phosphorylated. Earlier we have reviewed the data o n the structure and functions of tyrosine protein kinases [Mol. Biol., 27, 725-733 (1973)]. Here the functional significance and the structu re of protein phosphatases, which are antagonists of protein kinases, are considered.