Members of the 70-kilodalton heat shock protein family contain a highly conserved calmodulin-binding domain
Members of the 70-kilodalton heat shock protein family contain a highly conserved calmodulin-binding domain
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DOI：
10.1128/mcb.10.3.1234-1238.1990
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发表时间：
1990-03
影响因子：
5.3
通讯作者：
M. Stevenson;S. Calderwood
中科院分区：
文献类型：
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作者：
M. Stevenson;S. Calderwood
70千道尔顿热休克蛋白（hsp70）家族成员似乎是许多细胞蛋白质-蛋白质相互作用的重要组成部分。我们在这里报道了hsp70中一个新的功能区域的特征，这是一个钙调素结合位点。我们已经在hsp70蛋白中确定了一个包含钙调素结合域的21个氨基酸序列。肽形成一个潜在的两亲性α螺旋，并以高亲和力结合钙调蛋白。该钙调素结合序列与其他物种类似的hsp70序列的氨基酸同源性比较显示出高度的保守性。
The 70-kilodalton heat shock protein (hsp70) family members appear to be essential components in a number 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.