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The impact of exchanging the light and heavy chains on the structures of bovine ultralong antibodies.
- Source :
-
Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2024 Jul 01; Vol. 80 (Pt 7), pp. 154-163. Date of Electronic Publication: 2024 Jul 01. - Publication Year :
- 2024
-
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 β-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 1.6 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.<br /> (open access.)
- Subjects :
- Animals
Cattle
Crystallography, X-Ray
Amino Acid Sequence
Protein Conformation
Immunoglobulin Heavy Chains chemistry
Immunoglobulin Light Chains chemistry
Immunoglobulin Light Chains genetics
Complementarity Determining Regions chemistry
Immunoglobulin Fab Fragments chemistry
Models, Molecular
Subjects
Details
- Language :
- English
- ISSN :
- 2053-230X
- Volume :
- 80
- Issue :
- Pt 7
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology communications
- Publication Type :
- Academic Journal
- Accession number :
- 38958188
- Full Text :
- https://doi.org/10.1107/S2053230X2400606X