Computational modeling of full-length prochemerin from human

摘要

Chemerin is a protein bearing chemotaxis and anti-inflammation functions. Truncation of C-terminal region of chemerin precursor, prochemerin, regulates its activity. A reliable structure may help us understand the mechanism of such regulation. We model the full length prochemerin with a mixed strategy, that the cystatin-fold domain near the N-terminus is based on homology modeling of a template of cystatin, while the region near the C-terminus is built with ab initio modeling, involving docking, energy minimization, and molecular dynamics simulation. The resulted structure shows that the C-terminal region hinders residues Glu143 and Asp144 from interacting other molecules.