Backbone and methyl resonance assignments of the 42 kDa human Hsc70 nucleotide binding domain in the ADP state

被引：0

作者：

Erik R. P. Zuiderweg

Jason E. Gestwicki

机构：

[1] The University of Michigan Medical School,Department of Biological Chemistry

[2] University of California at San Francisco,Institute for Neurodegenerative Disease

来源：

Biomolecular NMR Assignments | 2017年 / 11卷

关键词：

Hsp70; Chaperones; Automatic assignments; Methyl reprotonation;

D O I：

暂无

中图分类号：

学科分类号：

摘要：

Hsc70 is the constitutively expressed mammalian heat shock 70 kDa (Hsp70) cytosolic chaperone. It plays a central role in cellular proteostasis and protein trafficking. Here, we present the backbone and methyl group assignments for the 386-residue nucleotide binding domain of the human protein. This domain controls the chaperone’s allostery, binds multiple co-chaperones and is the target of several classes of known chemical Hsp70 inhibitors. The NMR assignments are based on common triple resonance experiments with triple labeled protein, and on several 15N and 13C-resolved 3D NOE experiments with methyl-reprotonated samples. A combination of computer and manual data interpretation was used.

引用

页码：11 / 15

页数：4

共 42 条

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