The CDR1 of the human lambdaVI light chains adopts a new canonical structure.
We performed a comparative analysis of the conformation of the CDR1 of the human lambdaVI variable domains JTO and WIL and the equivalent loop of the lambdaI light chains RHE and KOL, which are representative of the type I canonical structure for lambda light chains. On the basis of the differences found in the main chain conformation, as well as the identity of the residues at key positions, we showed that the L1 of some lambdaVI light chains adopts a conformation that represents a new type of canonical structure. The conformation of the L1 of those lambdaVI light chains, is primarily determined by the presence of an Arg residue at position 25. The analysis of the lambdaVI light chain sequences so far reported, showed that near 25% of those proteins have Gly at position 25 instead of Arg, which represents an allotypic variant of the lambdaVI variable locus. The presence of Gly at position 25 in the L1 of lambdaVI light chains would imply a different conformation for this loop. Additionally, the position 68 in lambdaVI light chains, which is at the top of the FR3 loop, showed such spatial orientation and variability that suggested its participation in the conformation of the antigen recognition surface in this subgroup of lambda chains.
del Pozo Yauner
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L
Department of Molecular Medicine and Bioprocesses, Institute of Biotechnology, National Autonomous University of Mexico, Cuernavaca, Mexico.
Ortiz
E
E
Becerril
B
B
D000595:Amino Acid Sequence; D001324:Autoantigens; D030562:Databases, Protein; D006801:Humans; D046911:Macromolecular Substances / Q000737:chemistry; D008958:Models, Molecular; D009419:Nerve Tissue Proteins / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D016415:Sequence Alignment
D001324:Autoantigens; C063762:CDR1 protein, human; D046911:Macromolecular Substances; D009419:Nerve Tissue Proteins