PMID: 9530564Apr 8, 1998Paper

Progress in programming antibody fragments to crystallize

Immunotechnology : an International Journal of Immunological Engineering
A B Edmundson, C A Borrebaeck

Abstract

Completion of the X-ray analysis of the human B7-15A2 Fab opened a new vista (Immunotechnology 3, no. 4). In the crystal lattice, both the lambda-type light chain (CL domain) and gamma 1-type heavy chain (CH1 domain) participated in formation of antiparallel beta-pleated sheets with neighboring molecules related to the reference Fab by 2-fold axes. This observation evoked memories of the first description of this type of packing for human Bence-Jones (lambda chain) dimers 20 years ago (Ely K.R. et al. Biochemistry 1978;17:158-167). Reexamination of packing interactions in selected crystal systems revealed that the C domains of lambda and gamma 1 chains were structurally amenable to the formation of such cross-molecule beta-structures, but kappa chain CL domains were not. In the latter, a single proline residue disrupted the order of beta-strand 3-3 in the middle of the surface used in lambda and gamma 1 chains for intermolecular interactions with symmetry-related molecules. For the packing of Fv molecules, the VL domains are structurally well suited for analogous packing interactions through antiparallel 4-1 beta-strands in adjacent molecules. Such interactions have been shown to provide the driving force in the crystal packing...Continue Reading

References

Nov 5, 1992·Journal of Molecular Biology·Z C FanA B Edmundson
Feb 1, 1985·Molecular Immunology·K R ElyA B Edmundson
May 1, 1993·Proceedings of the National Academy of Sciences of the United States of America·L W GuddatA B Edmundson

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Citations

Nov 26, 2002·Journal of Molecular Recognition : JMR·Allen B Edmundson
Aug 9, 2018·Chemical Communications : Chem Comm·Luis M Blancas-MejiaMarina Ramirez-Alvarado
May 9, 2003·Protein Engineering·Christer WingrenCarl A K Borrebaeck

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