Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon

Article Abstract:

X-ray crystallography and cryo-electron microscopy were used to generate a three-dimensional structural model of an intact human rhinovirus 14 (HRV-14) complexed with Fab fragments (Fab17-IA). Contrary to popularly-held concepts of antibody neutralization, the Fab17-IA does not stimulate a conformational change in the HRV-14 capsid but, instead, it undergoes a large conformational change to accommodate the epitope. Moreover, the Fab17-IA tries to penetrate deep within the canyon in which the cellular receptor in HRV-14 binds.

Research, Models, Antigen-antibody reactions, Rhinoviruses

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Rad23 links DNA repair to the ubiquitin/proteasome pathway

Article Abstract:

The Rad23 evolutionarily conserved protein is important in nucleotide excision repair. A study shows that Rad23 interacts with the 26S proteasome via an amino-terminal ubiquitin-like domain (UblR23). A link is created between the DNA repair and proteasome pathways. It is thought that the ultraviolet sensitivity due to deletion of the UbLR23 domain, could be due to its lack of interaction with the proteasome.

Observations, DNA repair, Proteins

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Snapshots along the pathway

Article Abstract:

Protein crystallography has provided valuable information on the static structure of enzymes as well as defining substrate binding sites. A stud conducted by Bauke Djkstra showed that conventional crystallographic methods can monitor enzyme reactions. Moreover, sychroton radiation through diffraction data collection with the Laue method has made it possible to reduce sdata acquisition time.

Enzymes

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