Conformational heterogeneity in antibody-protein antigen recognition: implications for high affinity protein complex formation.

ABSTRACT: Specific, high affinity protein-protein interactions lie at the heart of many essential biological processes, including the recognition of an apparently limitless range of foreign proteins by natural antibodies, which has been exploited to develop therapeutic antibodies. To mediate biological processes, high affinity protein complexes need to form on appropriate, relatively rapid timescales, which presents a challenge for the productive engagement of complexes with large and complex contact surfaces (∼600-1800 Å(2)). We have obtained comprehensive backbone NMR assignments for two distinct, high affinity antibody fragments (single chain variable and antigen-binding (Fab) fragments), which recognize the structurally diverse cytokines interleukin-1β (IL-1β, β-sheet) and interleukin-6 (IL-6, α

SUBMITTER: Addis PW 

PROVIDER: S-EPMC3945379 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature