Professor Charlotte Deane, Department of Statistics, University of Oxford
Antibodies are a class of proteins indispensable for the vertebrate immune system. The general architecture of all antibodies is very similar, but they contain a hypervariable region which allows millions of antibody variants to exist, each of which can bind to different molecules. This binding malleability means that antibodies are an increasingly important category of biopharmaceuticals and biomarkers. In this talk I will present three of the tools we have developed that are part of our pathway for the rational design of antibodies. First SAbDab the Structural Antibody Database this is an online resource containing all the publicly available antibody structures annotated and presented in a consistent fashion. Second Abangle, this calculates the VH-VL orientation for any antibody and allows the comparison of these orientations with all other known structures. The binding site of an antibody is formed between the two variable domains, VH and VL, of its antigen binding fragment (Fab). Understanding how VH and VL orientate with respect to one another is important both for studying the mechanisms of antigen specificity and affinity and improving antibody modelling, docking and engineering. Finally Antibody i-Patch, this programme annotates the most likely antibody residues to be in contact with the antigen. Its residue predictions correlate with energetic importance and thus may be useful in guiding mutations in the artificial affinity maturation process. Using our predictions as constraints for a rigid-body docking algorithm, we are able to obtain high quality results in minutes. All of these tools are available from http://www.stats.ox.ac.uk/ research/proteins/resources.
Monday 21st October at 4.00 p.m. in Jennison Lecture Theatre