Role of the carboxyl terminus on the catalytic activity of protein kinase CK2α subunit

被引：12

作者：

Tapia, J ^{[1
]}

Jacob, G ^{[1
]}

Allende, CC ^{[1
]}

Allende, JE ^{[1
]}

机构：

[1] Univ Chile, Fac Med, Inst Ciencias Biomed, Programa Biol Celular & Mol, Santiago 7, Chile

来源：

FEBS LETTERS | 2002年 / 531卷 / 02期

基金：

英国惠康基金;

关键词：

casein kinase 2; deletions; mutations; protein structure; protein kinase domain;

D O I：

10.1016/S0014-5793(02)03555-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Protein kinase CK2 (also known as casein kinase 2) has catalytic (alpha, alpha') and regulatory (beta) subunits. The role of carboxyl amino acids in positions from 324 to 328 was studied for Xenopus laevis CK2alpha. Deletions and mutations of these residues were produced in recombinant CK2alpha, which was assayed for kinase activity. Activity dropped 7000-fold upon deletion of amino acids 324-328. The key residues are isoleucine 327 and phenylalanine 324. A three dimensional model of CK2alpha indicates that these hydrophobic residues of helix alphaN may interact with hydrophobic residues in helix alphaE which is linked to the catalytic center. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：363 / 368

页数：6

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