Structural highlights
Publication Abstract from PubMed
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 (1)H, (15)N, and (13)C chemical shift assignments at pH 6.0 and 25 degrees C, based on a uniformly doubly labelled (13)C/(15)N sample of the domain.
1H, 13C, and 15N resonance assignments of the N-terminal domain of human Tubulin Binding Cofactor C.,Garcia-Mayoral MF, Castano R, Zabala JC, Santoro J, Rico M, Bruix M Biomol NMR Assign. 2010 Oct;4(2):219-21. Epub 2010 Jul 9. PMID:20617401[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Garcia-Mayoral MF, Castano R, Zabala JC, Santoro J, Rico M, Bruix M. 1H, 13C, and 15N resonance assignments of the N-terminal domain of human Tubulin Binding Cofactor C. Biomol NMR Assign. 2010 Oct;4(2):219-21. Epub 2010 Jul 9. PMID:20617401 doi:10.1007/s12104-010-9250-9
