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Three-Dimensional Structure of the Fab′ Fragment of a Human Immunoglobulin at 2.8-Å Resolution
Open accessAbstract
The structure of the Fab′ fragment of a human myeloma immunoglobulin was determined by x-ray crystallographic analysis at 2.8-Å resolution. The Fourier map of the electron density was correlated with the aminoacid sequence to obtain a three-dimensional model. Four globular subunits, which correspond to the homology regions of the light and heavy chains, are arranged in a tetrahedral configuration. These subunits closely resemble each other, sharing a basic pattern of polypeptide chain folding. In each subunit, long sequences of tightly packed, hydrogen bonded polypeptide chain run parallel to the major axis of the subunit. No helical conformation can be seen. Different patterns of interchain disulfide linkage and unusual intrachain disulfide bonds that have been observed in other immunoglobulins can be explained with this model. The regions of hypervariable sequences in the light and heavy chains occur at one end of the molecule, in close spatial proximity.
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Citations
Cites
Wu, T. T., & Kabat, E. A. (1970) · The Journal of Experimental Medicine · doi:10.1084/jem.132.2.211 · Cited by 1,340
Cited by
Naturally occurring antibodies devoid of light chains
Hamers-Casterman, C., Atarhouch, T., Muyldermans, S., Robinson, G., Hammers, C., Songa, E. B., Bendahman, N., & Hammers, R. (1993) · Nature · doi:10.1038/363446a0 · Cited by 3,241
Replacing the complementarity-determining regions in a human antibody with those from a mouse
Jones, P. T., Dear, P. H., Foote, J., Neuberger, M. S., & Winter, G. (1986) · Nature · doi:10.1038/321522a0 · Cited by 1,406
Three-dimensional structure of an intact human immunoglobulin.
Silverton, E. W., Navia, M. A., & Davies, D. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.11.5140 · Cited by 375
Length distribution of CDRH3 in antibodies
Wu, T. T., Johnson, G., & Kabat, E. A. (1993) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340160102 · Cited by 284
Metadata
- Authors
- Poljak, R. J., Amzel, L. M., Avey, H. P., Chen, B. L., Phizackerley, R. P., & Saul, F.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1973-12
- Volume
- 70
- Issue
- 12
- Pages
- 3305-3310
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1984670732
- Cited by
- 384
- References
- 1
- FWCI
- 36.77
- Type
- journal article
- Language
- en
- Open access
- green
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- Poljak, R. J., Amzel, L. M., Avey, H. P., Chen, B. L., Phizackerley, R. P., & Saul, F. (1973). Three-Dimensional Structure of the Fab′ Fragment of a Human Immunoglobulin at 2.8-Å Resolution. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.70.12.3305
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
