|
|
|
Researchers have determined the structure of an enzyme that inactivates the nerve agent sarin and related toxic molecules. The results, published in the May issue of Nature Structural & Molecular Biology, provide insights into how the enzyme selects its targets and how this selectivity can be fine-tuned toward a particular set of targets.
Paraoxonase cleaves and inactivates toxic organophosphates such as sarin. It is also a component of the high-density lipoprotein particle (HDL, the 'good cholesterol') and its activity is involved in preventing the formation of fatty deposits on the artery walls. Paraoxonase is thus valuable from both antibioterrorism and medical perspectives. To understand how a single enzyme can act on such a broad spectrum of targets, Danny Tawfik and colleagues have determined the crystal structure of a mammalian paraoxonase. Structural and mutational analyses suggest the location of the active site and how the enzyme selects its targets. These results provide a basis for engineering the enzyme's activity toward a subset of its substrates for various biomedical applications. Author contact: Dan S. Tawfik
The Weizmann Institute of Science
Rehovot, Israel
Tel: +972 8 934 3637
E-mail: tawfik@weizmann.ac.il Also available online. (C) Nature Structural & Molecular Biology press release.
Message posted by: Trevor M. D'Souza
|
|
Variants Associated with Pediatric Allergic Disorder
Mutations in PHF6 Found in T-Cell Leukemia
Genetic Risk Variant for Urinary Bladder Cancer
Antibody Has Therapeutic Effect on Mice with ALS
Regulating P53 Activity in Cancer Cells
Anti-RNA Therapy Counters Breast Cancer Spread
Mitochondrial DNA Diversity
The Power of RNA Sequencing
‘Pro-Ageing' Therapy for Cancer?
Niche Genetics Influence Leukaemia
Molecular Biology: Clinical Promise for RNA Interference
Chemoprevention Cocktail for Colon Cancer
more news ...
|