Ontology highlight
ABSTRACT:
SUBMITTER: Khan MI
PROVIDER: S-EPMC6380570 | biostudies-literature | 2019
REPOSITORIES: biostudies-literature
Khan Md Imran MI Yuan Tai T Chou Ruey-Hwang RH Yu Chin C
PloS one 20190219 2
The Ca2+-dependent human S100A4 (Mts1) protein is part of the S100 family. Here, we studied the interactions of S100A4 with S100A1 using nuclear magnetic resonance (NMR) spectroscopy. We used the chemical shift perturbed residues from HSQC to model S100A4 and S100A1 complex with HADDOCK software. We observed that S100A1 and the RAGE V domain have an analogous binding area in S100A4. We discovered that S100A4 acts as an antagonist among the RAGE V domain and S100A1, which inhibits tumorigenesis a ...[more]