The less conserved metal-binding site in human CRISP1 remains sensitive to zinc ions to permit protein oligomerization.

ABSTRACT: Cysteine-rich secretory proteins (CRISPs) are a subgroup of the CRISP, antigen 5 and PR-1 (CAP) superfamily that is characterized by the presence of a conserved CAP domain. Two conserved histidines in the CAP domain are proposed to function as a Zn²⁺-binding site with unknown function. Human CRISP1 is, however, one of the few family members that lack one of these characteristic histidine residues. The Zn²⁺-dependent oligomerization properties of human CRISP1 were investigated using a maltose-binding protein (MBP)-tagging approach in combination with low expression levels in XL-1 Blue bacteria. Moderate yields of soluble recombinant MBP-tagged human CRISP1 (MBP-CRISP1) and the MBP-tagged CAP domain of CRISP1 (MBP-CRISP1^ΔC) were obtained. Zn²⁺ spec

SUBMITTER: Sheng J 

PROVIDER: S-EPMC7943821 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature