Antibody CDR loops as ensembles in solution vs. canonical clusters from X-ray structures.

ABSTRACT: In the past decade, the relevance of antibodies as therapeutics has increased substantially. Therefore, structural and functional characterization, in particular of the complementarity-determining regions (CDRs), is crucial to the design and engineering of antibodies with unique binding properties. Various studies have focused on classifying the CDR loops into a small set of main-chain conformations to facilitate antibody design by assuming that certain sequences can only adopt a limited number of conformations. Here, we present a kinetic classification of CDR loop structures as ensembles in solution. Using molecular dynamics simulations in combination with strong experimental structural information, we observe conformational transitions between canonical clusters and additional dominant s

SUBMITTER: Fernandez-Quintero ML 

PROVIDER: S-EPMC7153821 | biostudies-literature | 2020 Jan-Dec

REPOSITORIES: biostudies-literature