Structural evidence for a constrained conformation of short CDR‐L3 in antibodies
- 27 January 2014
- journal article
- structure note
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 82 (8) , 1679-1683
- https://doi.org/10.1002/prot.24522
Abstract
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; 82:1679–1683.Keywords
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