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
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
收藏
页码:219 / 221
页数:3
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