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

ABSTRACT

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 ß-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.