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Conformation of complementarity determining region L1 loop in murine IgG lambda light chain extends the repertoire of
1Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec.
The refined structure of Se155-4 Fab fragment, the first murine antibody with the lambda light chain, reveals a novel conformation of the light chain complementarity determining region L1. This conformation extends the repertoire of canonical structures. The main determinant of this conformation is the packing of the Val27c side-chain into a hydrophobic pocket formed by the side-chains of Ala33, Leu66, Ala71 and Leu90. The framework L-FR3 loop, encompassing residues 66 to 72, which packs next to the L1 loop, bends significantly more toward the exterior of the molecule than in other Fab fragments. Sequence analysis suggests that the conformations of the L1 and L-FR3 loops observed in Se155-4 are adopted by a majority of murine lambda light chains.
The refined structure of Se155-4 Fab fragment, the first murine antibody with the lambda light chain, reveals a novel conformation of the light chain complementarity determining region L1. This conformation extends the repertoire of canonical structures. The main determinant of this conformation is the packing of the Val27c side-chain into a hydrophobic pocket formed by the side-chains of Ala33, Leu66, Ala71 and Leu90. The framework L-FR3 loop, encompassing residues 66 to 72, which packs next to the L1 loop, bends significantly more toward the exterior of the molecule than in other Fab fragments. Sequence analysis suggests that the conformations of the L1 and L-FR3 loops observed in Se155-4 are adopted by a majority of murine lambda light chains.