Journal of molecular biology, 2006-04, Vol.357 (5), p.1566-1574
2006
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Details
- Autor(en) / Beteiligte
- Titel
- Antibody Elbow Angles are Influenced by their Light Chain Class
- Ist Teil von
- Journal of molecular biology, 2006-04, Vol.357 (5), p.1566-1574
- Ort / Verlag
- England: Elsevier Ltd
- Erscheinungsjahr
- 2006
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0022-2836eISSN: 1089-8638DOI: 10.1016/j.jmb.2006.01.023Titel-ID: cdi_proquest_miscellaneous_67798390
- Format
- –
- Schlagworte
- 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