A single residue switch reveals principles of antibody domain integrity.

ABSTRACT: Despite their importance for antibody architecture and design, the principles governing antibody domain stability are still not understood in sufficient detail. Here, to address this question, we chose a domain from the invariant part of IgG, the C_H2 domain. We found that compared with other Ig domains, the isolated C_H2 domain is a surprisingly unstable monomer, exhibiting a melting temperature of ∼44 °C. We further show that the presence of an additional C-terminal lysine in a C_H2 variant substantially increases the melting temperature by ∼14 °C relative to C_H2 WT. To explore the molecular mechanism of this effect, we employed biophysical approaches to probe structural features of C_H2. The results revealed that Lys¹⁰¹ is ke

SUBMITTER: Weber B 

PROVIDER: S-EPMC6222096 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature