Modelling study of dimerization in mammalian defensins.

ABSTRACT:

Background

Defensins are antimicrobial peptides of innate immunity functioning by non-specific binding to anionic phospholipids in bacterial membranes. Their cationicity, amphipathicity and ability to oligomerize are considered key factors for their action. Based on structural information on human beta-defensin 2, we examine homologous defensins from various mammalian species for conserved functional physico-chemical characteristics.

Results

Based on homology greater than 40%, structural models of 8 homologs of HBD-2 were constructed. A conserved pattern of electrostatics and dynamics was observed across 6 of the examined defensins; models backed by energetics suggest that the defensins in these 6 organisms are characterized by dimerization-linked enhanced functional potenti

SUBMITTER: Suresh A 

PROVIDER: S-EPMC1764473 | biostudies-literature | 2006 Dec

REPOSITORIES: biostudies-literature