Probing the Impact of Local Structural Dynamics of Conformational Epitopes on Antibody Recognition.

ABSTRACT: Antibody-antigen interactions are governed by recognition of specific residues and structural complementarity between the antigen epitope and antibody paratope. While X-ray crystallography has provided detailed insights into static conformations of antibody-antigen complexes, factors such as conformational flexibility and dynamics, which are not readily apparent in the structures, can also have an impact on the binding event. Here we investigate the contribution of dynamics in the HIV-1 gp120 glycoprotein to antibody recognition of conserved conformational epitopes, including the CD4- and coreceptor-binding sites, and an inner domain site that is targeted by ADCC-active antibodies. Hydrogen/deuterium-exchange mass spectrometry (HDX-MS) was used to measure local structural dynamics across a

SUBMITTER: Liang Y 

PROVIDER: S-EPMC5479570 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature