Antibody elbow angles are influenced by their light chain class

J Mol Biol. 2006 Apr 14;357(5):1566-74. doi: 10.1016/j.jmb.2006.01.023. Epub 2006 Jan 25.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Antibodies / chemistry*
  • Antibodies / metabolism
  • Immunoglobulin Fab Fragments / chemistry
  • Immunoglobulin Fab Fragments / metabolism
  • Immunoglobulin Light Chains / chemistry*
  • Immunoglobulin Light Chains / classification*
  • Immunoglobulin Light Chains / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation*
  • Software


  • Antibodies
  • Immunoglobulin Fab Fragments
  • Immunoglobulin Light Chains