Solution structure and mapping of a very weak calcium-binding site of human translationally controlled tumor protein by NMR

Arch Biochem Biophys. 2007 Nov 1;467(1):48-57. doi: 10.1016/j.abb.2007.08.021. Epub 2007 Aug 30.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Biomarkers, Tumor / chemistry*
  • Biomarkers, Tumor / physiology*
  • Calcium / chemistry*
  • Humans
  • Kinetics
  • Magnetic Resonance Spectroscopy / methods*
  • Molecular Conformation
  • Molecular Sequence Data
  • Neoplasm Proteins / chemistry*
  • Neoplasms / metabolism*
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Secondary
  • Sequence Homology, Amino Acid
  • Tumor Protein, Translationally-Controlled 1

Substances

  • Biomarkers, Tumor
  • Neoplasm Proteins
  • TPT1 protein, human
  • Tumor Protein, Translationally-Controlled 1
  • Calcium