Welcome to the Department of Biochemistry, part of the University of Oxford's Medical Sciences Division. We are one of the largest Biochemistry departments in the world and carry out world-class research and teaching. Our researchers come from a range of disciplines and work in a collaborative environment on all aspects of modern molecular and cellular biochemistry. We hope you enjoy reading more about our activities on these pages.
Professor Mark Sansom, Head of Department
Enzyme structure offers new hopes for better antivirals
The structure of a cellular enzyme that is crucial for the survival of many pathogenic viruses has been solved in a new study.
Crystal structure of mouse α-glucosidase II in cartoon representation.
Nicole Zitzmann and members of her team, together with colleagues from Italy and France, have published their findings in PNAS (1). Their work on the enzyme, a key component of the quality control machinery that ensures that glycoproteins fold properly, opens the way for the development of potent and selective antivirals against a range of deadly diseases.
Proteins of all the major human pathogenic viruses, including Zika, dengue, influenza and Ebola, are dependent upon the host cell machinery that controls glycoproteins passing through the endoplasmic reticulum (ER). After the glycoprotein enters the ER, whether it is viral or cellular, it passes through a set of enzymes that modify its glycan chains and help it to fold properly. This is known as the calnexin cycle - calnexin, a component of the cycle, is a lectin that holds the glycoprotein so that it can fold properly. If the glycoprotein is not correctly folded on its first cycle, it must pass round the cycle again. ER α-glucosidase I and II (α-GluI and α-GluII), which sequentially remove glucose from N-linked glycans on glycoproteins, and UGGT, are the main enzymatic players in the cycle.