Molecular mechanism of calcium induced trimerization of C1q-like domain of otolin-1 from human and zebrafish.

ABSTRACT: The C1q superfamily includes proteins involved in innate immunity, insulin sensitivity, biomineralization and more. Among these proteins is otolin-1, which is a collagen-like protein that forms a scaffold for the biomineralization of inner ear stones in vertebrates. The globular C1q-like domain (gC1q), which is the most conserved part of otolin-1, binds Ca²⁺ and stabilizes its collagen-like triple helix. The molecular details of the assembly of gC1q otolin-1 trimers are not known. Here, we substituted putative Ca²⁺-binding acidic residues of gC1q otolin-1 with alanine to analyse how alanine influences the formation of gC1q trimers. We used human and zebrafish gC1q otolin-1 to assess how evolutionary changes affected the function of the protein. Surprisingly, the mutat

SUBMITTER: Holubowicz R 

PROVIDER: S-EPMC8211825 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature