Antibody elbow angles are influenced by their light chain class.
We have examined the elbow angles for 365 different Fab fragments, and observe that Fabs with lambda light chains have adopted a wider range of elbow angles than their kappa chain counterparts, and that the lambda light chain Fabs are frequently found with very large (>195 degrees ) elbow angles. This apparent hyperflexibility of lambda chain Fabs may be due to an insertion in their switch region, which is one residue longer than in kappa chains, with glycine occurring most frequently at the insertion position. A new, web-based computer program that was used to calculate the Fab elbow angles is described.
Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92037, USA. robyn@scripps.edu
Robyn L
RL
Stanfield
Adam
A
Zemla
Ian A
IA
Wilson
Bernhard
B
Rupp
D000906:Antibodies / Q000737:chemistry* / Q000378:metabolism; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry / Q000378:metabolism; D007147:Immunoglobulin Light Chains / Q000737:chemistry* / Q000145:classification* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012984:Software
D000906:Antibodies; D007140:Immunoglobulin Fab Fragments; D007147:Immunoglobulin Light Chains