| Article ID | Journal | Published Year | Pages | File Type | 
|---|---|---|---|---|
| 8292068 | Archives of Biochemistry and Biophysics | 2007 | 10 Pages | 
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 β-sheet, which shows a conserved fold in the TCTP family. The C-terminal portions of loop Lα3β8 and strand β9 and the N-terminal region of strand β8 may form a calcium-binding site in the human TCTP structure, which is largely conserved in the sequence alignment of TCTPs. The Kd value for the calcium binding is 0.022-0.025 M indicating a very weak calcium-binding site.
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											Authors
												Yingang Feng, Dongsheng Liu, Hongwei Yao, Jinfeng Wang, 
											