Toward an understanding of the conformational plasticity of S100A8 and S100A9 Ca²⁺-binding proteins.

ABSTRACT: S100A8 and S100A9 are small, human, Ca²⁺-binding proteins with multiple intracellular and extracellular functions in signaling, regulation, and defense. The two proteins are not detected as monomers but form various noncovalent homo- or hetero-oligomers related to specific activities in human physiology. Because of their significant roles in numerous medical conditions, there has been intense research on the conformational properties of various S100A8 and S100A9 proteoforms as essential targets of drug discovery. NMR or crystal structures are currently available only for mutated or truncated protein complexes, mainly with bound metal ions, that may well reflect the proteins' properties outside cells but not in other biological contexts in which they perform. Here, we used struct

SUBMITTER: Polakowska M 

PROVIDER: S-EPMC10124908 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature