Feng Yingang, Liu Dongsheng, Yao Hongwei, Wang Jinfeng
National Laboratory of Biomacromolecules, Center for Structural and Molecular Biology, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China.
Arch Biochem Biophys. 2007 Nov 1;467(1):48-57. doi: 10.1016/j.abb.2007.08.021. Epub 2007 Aug 30.
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.
人翻译调控肿瘤蛋白（TCTP）是一种与生长相关的钙结合蛋白。我们测定了人TCTP的溶液结构和主链动力学，并使用多维核磁共振波谱法确定了人TCTP的钙结合位点。人TCTP的整体结构具有一个相当刚性的折叠良好的核心和一个通过短的双链β-折叠连接的非常灵活的长环，这在TCTP家族中显示出保守的折叠。环L（α3β8）的C末端部分、链β9以及链β8的N末端区域可能在人TCTP结构中形成一个钙结合位点，该位点在TCTP的序列比对中基本保守。钙结合的K(d)值为0.022 - 0.025 M，表明这是一个非常弱的钙结合位点。
