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Antibody elbow angles are influenced by their light chain class

Academic Article
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Overview

authors

  • Stanfield, Robyn
  • Zemla, A.
  • Wilson, Ian
  • Rupp, B.

publication date

  • April 2006

journal

  • Journal of Molecular Biology  Journal

abstract

  • 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.

subject areas

  • Antibodies
  • Immunoglobulin Fab Fragments
  • Immunoglobulin Light Chains
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Software
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Research

keywords

  • antibody
  • computer program
  • elbow angle
  • kappa
  • lambda
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/j.jmb.2006.01.023

PubMed ID

  • 16497332
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Additional Document Info

start page

  • 1566

end page

  • 1574

volume

  • 357

issue

  • 5

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