S100A6 is involved in several vital biological functions, such as calcium
sensing and cell proliferation. It is a homodimeric protein that belongs to the
S100 protein family. The receptor for advanced glycation end products (RAGE) has
been shown to play a role in the progression of various disease conditions, such
as diabetes and immune/inflammatory disorders. Information regarding the
association of RAGE with S100 proteins at a molecular level is useful to
understand the diversity of the RAGE signaling pathways. In this report,
biomolecular NMR techniques were utilized for the resonance assignment of the
C3S mutation in human S100A6 and characterizing its interaction with the RAGE V
domain. Further binding affinity between S100A6m and the RAGE V domain was
determined by isothermal titration calorimetric studies. HADDOCK was used to
generate a heterotetramer model of the S100A6m-RAGE V domain complex. This model
provides an important insights into the S100-RAGE cellular signaling pathway.
