Abstract
Human S100A11 is a homodimeric EF-hand calcium binding protein that undergoes a calcium-induced conformational change and interacts with target protein. RAGE is a multiligand receptor binding to S100A11 and the interactions at molecular level have not been reported. It is a member of the immunoglobulin protein family of cell surface molecules. RAGE plays an important role in many human pathologies by inducing cellular signaling actions upon binding of different ligands. In chapter 2, we purified human S100A11 and RAGE V by using phenyl-sepharose column and cobalt affinity column. In chapter 3 and 4, chemical shift assignments were made from HNCA, HN(CO)CA, HCCH-TOCST and HCCH-COSY,etc. Furthermore, the solution structure of human calcium bound S100A11 was determined by ARIA/CNS software using the experimental restraints such as distance, dihedral angle, hydrogen bond. In chapter 5, we used a variety of biophysical methods, including 2D 1H-15N HSQC titration, fluorescence spectroscopy and analytical ultracentrifugation, to characterize the binding interface regions and interactions between S100A11 and RAGE at the molecular level. Finally, we postulate that S100A11 and RAGE might interact with each other.