TB & Outbreaks Week
Welcome to NewsRx!
Learn more about a six-week, no-risk free trial of TB & Outbreaks Week
We're a pay-per-view site for premium content. If you'd like to purchase this article, it's only $3.00.
Life Sciences
Investigators at University of Limerick zero in on life sciences
June 17th, 2008
According to recent research from Limerick, Ireland, "OpcA is an integral outer membrane adhesin protein from Neisseria meningitidis, the causative agent of meningococcal meningitis and septicemia. It binds to sialic acid (SA)-containing polysaccharides on the surface of epithelial cells." "The crystal structure of OpcA showed that the protein adopts a 10-stranded beta-barrel structure, with five extensive loop regions on the extracellular side of the membrane. These form a crevice structure, lined with basic residues, which was hypothesized to act as the binding site for polysaccharide ligands. In the current study, a distinctly different OpcA structure has been...
Source: TB & Outbreaks Week (2008-06-17)
|