Investigating Native Metal Ion Binding Sites in Mammalian Histidine-Rich Glycoprotein.

ABSTRACT: Mammalian histidine-rich glycoprotein (HRG) is a highly versatile and abundant blood plasma glycoprotein with a diverse range of ligands that is involved in regulating many essential biological processes, including coagulation, cell adhesion, and angiogenesis. Despite its biomedical importance, structural information on the multi-domain protein is sparse, not least due to intrinsically disordered regions that elude high-resolution structural characterization. Binding of divalent metal ions, particularly Zn^II, to multiple sites within the HRG protein is of critical functional importance and exerts a regulatory role. However, characterization of the Zn^II binding sites of HRG is a challenge; their number and composition as well as their affinities and stoichiometries of

SUBMITTER: Ackermann K 

PROVIDER: S-EPMC10103162 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature