1H, 13C, and 15N resonance assignments of the N-terminal domain of human Tubulin Binding Cofactor C.
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 α and β-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 (1)H, (15)N, and (13)C chemical shift assignments at pH 6.0 and 25°C, based on a uniformly doubly labelled (13)C/(15)N sample of the domain.
García-Mayoral
M F
MF
Departamento de Química Física Biológica, Instituto de Química Física Rocasolano, CSIC, Serrano 119, 28006, Madrid, Spain.
Castaño
R
R
Zabala
J C
JC
Santoro
J
J
Rico
M
M
Bruix
M
M
D002247:Carbon Isotopes; D006801:Humans; D006859:Hydrogen; D018832:Molecular Chaperones / Q000737:chemistry*; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D002247:Carbon Isotopes; D018832:Molecular Chaperones; D009587:Nitrogen Isotopes; C455270:tubulin-specific chaperone C; D006859:Hydrogen