MEMBERS OF THE 70-KILODALTON HEAT-SHOCK PROTEIN FAMILY CONTAIN A HIGHLY CONSERVED CALMODULIN-BINDING DOMAIN

被引：123

作者：

STEVENSON, MA ^{[1
]}

CALDERWOOD, SK ^{[1
]}

机构：

[1] HARVARD UNIV,SCH MED,JOINT CTR RADIAT THERAPY,BOSTON,MA 02115

来源：

MOLECULAR AND CELLULAR BIOLOGY | 1990年 / 10卷 / 03期

关键词：

D O I：

10.1128/MCB.10.3.1234

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：

The 70-kilodalton heat shock protein (hsp70) family members appear to be essential components in a number of cellular protein-protein interactions. We report here on the characterization of a new functional region in hsp70, a calmodulin-binding site. We have identified a 21-amino-acid sequence within the hsp70 protein that contains a calmodulin-binding domain. The peptide formed a potential amphipathic alpha helix and bound calmodulin with high affinity. Comparison of amino acid homology of this calmodulin-binding sequence with analogous hsp70 sequences from other species showed a high degree of conservation.

引用

页码：1234 / 1238

页数：5

共 35 条

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