A copy of this work was available on the public web and has been preserved in the Wayback Machine. The capture dates from 2018; you can also visit the original URL.
The file type is
S100A6 and S100A11 Are Specific Targets of the Calcium- and Zinc-binding S100B Proteinin Vivo
Journal of Biological Chemistry
In solution, S100B protein is a noncovalent homodimer composed of two subunits associated in an antiparallel manner. Upon calcium binding, the conformation of S100B changes dramatically, leading to the exposure of hydrophobic residues at the surface of S100B. The residues in the C-terminal domain of S100B encompassing Phe 87 and Phe 88 have been implicated in interaction with target proteins. In this study, we used two-hybrid technology to identify specific S100B target proteins. Using S100B asdoi:10.1074/jbc.m003943200 pmid:10913138 fatcat:o2e4x33erfau3k7cbyub43oa2q