Structural highlights
Publication Abstract from PubMed
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. (c) 2014 Wiley Periodicals, Inc.
Structural evidence for a constrained conformation of short CDR-L3 in antibodies.,Teplyakov A, Obmolova G, Malia TJ, Luo J, Gilliland GL Proteins. 2014 Jan 27. doi: 10.1002/prot.24522. PMID:24470236[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Teplyakov A, Obmolova G, Malia TJ, Luo J, Gilliland GL. Structural evidence for a constrained conformation of short CDR-L3 in antibodies. Proteins. 2014 Jan 27. doi: 10.1002/prot.24522. PMID:24470236 doi:http://dx.doi.org/10.1002/prot.24522
