The impact of exchanging the light and heavy chains on the structures of bovine ultralong antibodies.
Acta Crystallogr F Struct Biol Commun
; 80(Pt 7): 154-163, 2024 Jul 01.
Article
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| MEDLINE
| ID: mdl-38958188
ABSTRACT
The third complementary-determining regions of the heavy-chain (CDR3H) variable regions (VH) of some cattle antibodies are highly extended, consisting of 48 or more residues. These `ultralong' CDR3Hs form ß-ribbon stalks that protrude from the surface of the antibody with a disulfide cross-linked knob region at their apex that dominates antigen interactions over the other CDR loops. The structure of the Fab fragment of a naturally paired bovine ultralong antibody (D08), identified by single B-cell sequencing, has been determined to 1.6â
Å resolution. By swapping the D08 native light chain with that of an unrelated antigen-unknown ultralong antibody, it is shown that interactions between the CDR3s of the variable domains potentially affect the fine positioning of the ultralong CDR3H; however, comparison with other crystallographic structures shows that crystalline packing is also a major contributor. It is concluded that, on balance, the exact positioning of ultralong CDR3H loops is most likely to be due to the constraints of crystal packing.
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MEDLINE
Asunto principal:
Fragmentos Fab de Inmunoglobulinas
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Modelos Moleculares
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Cadenas Pesadas de Inmunoglobulina
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Cadenas Ligeras de Inmunoglobulina
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Regiones Determinantes de Complementariedad
Idioma:
En
Revista:
Acta Crystallogr F Struct Biol Commun
Año:
2024
Tipo del documento:
Article