A molecular dynamics study of reovirus attachment protein sigma1 reveals conformational changes in sigma1 structure.

ABSTRACT: Molecular dynamics simulations were performed using the recently determined crystal structure of the reovirus attachment protein, sigma1. These studies were conducted to improve an understanding of two unique features of sigma1 structure: the protonation state of Asp(345), which is buried in the sigma1 trimer interface, and the flexibility of the protein at a defined region below the receptor-binding head domain. Three copies of aspartic acids Asp(345) and Asp(346) cluster in a solvent-inaccessible and hydrophobic region at the sigma1 trimer interface. These residues are hypothesized to mediate conformational changes in sigma1 during viral attachment or cell entry. Our results indicate that protonation of Asp(345) is essential to the integrity of the trimeric structure seen by x-ray crysta

SUBMITTER: Cavalli A 

PROVIDER: S-EPMC1304249 | biostudies-literature | 2004 Jun

REPOSITORIES: biostudies-literature