1H, 13C, and 15N resonance assignments of the N-terminal domain of human Tubulin Binding Cofactor C

被引：2

作者：

Garcia-Mayoral, M. F. ^{[1
]}

Castano, R. ^{[2
]}

Zabala, J. C. ^{[2
]}

Santoro, J. ^{[1
]}

Rico, M. ^{[1
]}

Bruix, M. ^{[1
]}

机构：

[1] CSIC, Inst Quim Fis Rocasolano, Dept Quim Fis Biol, E-28006 Madrid, Spain

[2] Univ Cantabria, Dept Biol Mol, Inst Formac & Invest Marques Valdecilla, Fac Med, Santander 39011, Spain

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2010年 / 4卷 / 02期

关键词：

Tubulin binding cofactor C; Centrosome; NMR resonance assignment; Secondary structure;

D O I：

10.1007/s12104-010-9250-9

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

Human Tubulin Binding Cofactor C (hTBCC) is a 346 amino acid protein composed of two domains, which is involved in the folding pathway of newly synthesized alpha and beta-tubulins. The 3D structure of the 111-residue hTBCC N-terminal domain of the protein has not yet been determined. As a previous step to that end, here we report the NMR H-1, N-15, and C-13 chemical shift assignments at pH 6.0 and 25A degrees C, based on a uniformly doubly labelled C-13/N-15 sample of the domain.

引用

页码：219 / 221

页数：3

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