Insights into the structure and dynamics of lysyl oxidase propeptide, a flexible protein with numerous partners.

ABSTRACT: Lysyl oxidase (LOX) catalyzes the oxidative deamination of lysine and hydroxylysine residues in collagens and elastin, which is the first step of the cross-linking of these extracellular matrix proteins. It is secreted as a proenzyme activated by bone morphogenetic protein-1, which releases the LOX catalytic domain and its bioactive N-terminal propeptide. We characterized the recombinant human propeptide by circular dichroism, dynamic light scattering, and small-angle X-ray scattering (SAXS), and showed that it is elongated, monomeric, disordered and flexible (D_max: 11.7 nm, R_g: 3.7 nm). We generated 3D models of the propeptide by coarse-grained molecular dynamics simulations restrained by SAXS data, which were used for docking experiments. Furthermore, we have identi

SUBMITTER: Vallet SD 

PROVIDER: S-EPMC6078952 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature