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Updated: Jul 11, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Solution structure and mapping of a very weak calcium-binding site of human translationally controlled tumor protein
Yingang Feng1, Dongsheng Liu, Hongwei Yao
1National Laboratory of Biomacromolecules, Center for Structural and Molecular Biology, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China.
Abstract:
Human translationally controlled tumor protein (TCTP) is a growth-related, calcium-binding protein. We determined the solution structure and backbone dynamics of human TCTP, and identified the calcium-binding site of human TCTP using multi-dimensional NMR spectroscopy. The overall structure of human TCTP has a rather rigid well-folded core and a very flexible long loop connected by a short two-strand beta-sheet, which shows a conserved fold in the TCTP family. The C-terminal portions of loop L(alpha3beta8) and strand beta9 and the N-terminal region of strand beta8 may form a calcium-binding site in the human TCTP structure, which is largely conserved in the sequence alignment of TCTPs. The K(d) value for the calcium binding is 0.022-0.025 M indicating a very weak calcium-binding site.
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