Professor Philip Biggin
Biochemistry
University of Oxford
Oxford, England

Monday, April 12, 2021
3:00 pm (CT)
Zoom webinar recording

Abstract

Protein synthesis in the endoplasmic reticulum of eukaryotic cells requires a high concentration of luminal chaperones to function. However, these chaperones are frequently swept along the secretory pathway and must be retrieved to maintain the viability of the cell. This selective retrieval system must transport proteins of widely differing abundance and also recognize the signal against the backdrop of an extremely crowded environment. The best characterized system is the KDEL-retrieval system, which captures escaped ER proteins with a KDEL or variant C-terminal signal at acidic pH in the Golgi, and releases them at neutral pH in the ER. The structure of the KDEL receptor was recently solved and provided some important information about how this system functions. However, there remain many aspects that the structure alone does not address. In this talk I will primarily outline computational approaches we have used to address some outstanding questions, including amongst other things the basis for signal selectivity. I will also highlight the role of an unusually short hydrogen-bond and waters within the pocket.

Please click the link below to join the webinar: https://illinois.zoom.us/j/86157513673? pwd=cXpacnUzL1JyOGpZS25lODZieUVrZz09 Password: 360579