Divalent metal binding by histidine‐rich glycoprotein differentially regulates higher order oligomerisation and proteolytic processing

The serum protein histidine‐rich glycoprotein ( HRG ) has been implicated in tissue injury and tumour growth. Several HRG functions are regulated by the divalent metal Zn 2+ , including ligand binding and proteolytic processing that releases active HRG fragments. Although HRG can bind divalent metals other than Zn 2+ , the impact of these divalent metals on the biophysical properties of HRG remains poorly understood. We now show that HRG binds...