Antibody elbow angles are influenced by their light chain class

RL Stanfield, A Zemla, IA Wilson, B Rupp - Journal of molecular biology, 2006 - Elsevier
RL Stanfield, A Zemla, IA Wilson, B Rupp
Journal of molecular biology, 2006Elsevier
We have examined the elbow angles for 365 different Fab fragments, and observe that Fabs
with λ light chains have adopted a wider range of elbow angles than their κ chain
counterparts, and that the λ light chain Fabs are frequently found with very large (> 195°)
elbow angles. This apparent hyperflexibility of λ chain Fabs may be due to an insertion in
their switch region, which is one residue longer than in κ chains, with glycine occurring most
frequently at the insertion position. A new, web-based computer program that was used to …
We have examined the elbow angles for 365 different Fab fragments, and observe that Fabs with λ light chains have adopted a wider range of elbow angles than their κ chain counterparts, and that the λ light chain Fabs are frequently found with very large (>195°) elbow angles. This apparent hyperflexibility of λ chain Fabs may be due to an insertion in their switch region, which is one residue longer than in κ 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.
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