Length-independent structural similarities enrich the antibody CDR canonical class model.

ABSTRACT: Complementarity-determining regions (CDRs) are antibody loops that make up the antigen binding site. Here, we show that all CDR types have structurally similar loops of different lengths. Based on these findings, we created length-independent canonical classes for the non-H3 CDRs. Our length variable structural clusters show strong sequence patterns suggesting either that they evolved from the same original structure or result from some form of convergence. We find that our length-independent method not only clusters a larger number of CDRs, but also predicts canonical class from sequence better than the standard length-dependent approach. To demonstrate the usefulness of our findings, we predicted cluster membership of CDR-L3 sequences from 3 next-generation sequencing datasets of the ant

SUBMITTER: Nowak J 

PROVIDER: S-EPMC4966832 | biostudies-literature | 2016 May-Jun

REPOSITORIES: biostudies-literature