Antibody Elbow Angles are Influenced by their Light Chain Class

• Published in: Journal of molecular biology Vol. 357; no. 5; pp. 1566 - 1574
• Main Authors: Stanfield, Robyn L., Zemla, Adam, Wilson, Ian A., Rupp, Bernhard
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 14-04-2006
• Subjects: Antibodies - chemistry; Antibodies - metabolism; antibody; computer program; elbow angle; Immunoglobulin Fab Fragments - chemistry; Immunoglobulin Fab Fragments - metabolism; Immunoglobulin Light Chains - chemistry; Immunoglobulin Light Chains - classification; Immunoglobulin Light Chains - metabolism; kappa; lambda; Models, Molecular; Molecular Sequence Data; Protein Conformation; Software; elbow angle; lambda; POB; antibody; V L; C H1; computer program; kappa; V H; C L
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1016/j.jmb.2006.01.023

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.