Structural evidence for a constrained conformation of short CDR-L3 in antibodies
Article first published online: 18 FEB 2014
Copyright © 2014 Wiley Periodicals, Inc.
Proteins: Structure, Function, and Bioinformatics
How to Cite
Teplyakov, A., Obmolova, G., Malia, T. J., Luo, J. and Gilliland, G. L. (2014), Structural evidence for a constrained conformation of short CDR-L3 in antibodies. Proteins. doi: 10.1002/prot.24522
- Article first published online: 18 FEB 2014
- Accepted manuscript online: 27 JAN 2014 07:07AM EST
- Manuscript Accepted: 16 JAN 2014
- Manuscript Revised: 29 DEC 2013
- Manuscript Received: 6 DEC 2013
- crystal structure;
- canonical structure;
- induced fit;
- microseed matrix screening
Three Fab structures used as targets in the Antibody Modeling Assessment presented a challenge for modeling CDR-L3 due to deviations from the most typical canonical structure. In all three antibodies CDR-L3 has eight residues, which is one residue shorter than usual, and has a conformation that is rarely observed in crystal structures. We analyzed the sequence and structural determinants of this conformation and found that the “short” CDR-L3 is remarkably rigid and retains the conformation in the interactions with antigens and neighboring CDRs. Proteins 2014. © 2014 Wiley Periodicals, Inc.