The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Crystallographic structure of an intact IgG1 monoclonal antibody 1 1Edited by I. A. Wilson
Open accessAbstract
The structure of an intact monoclonal antibody for phenobarbital, subclass IgG1, has been determined to 3.2 A resolution by X-ray crystallography. The molecule was visualized in a monoclinic unit cell having an entire immunoglobulin as the asymmetric unit. The two Fab segments, both with elbow angles of 155 degrees , were related by a rotation of 179.7 degrees plus a translation along the approximate dyad of 9 A. This is the first observation of such an Fab translation in a structurally defined antibody. The approximate 2-fold of the Fc was independent of that relating Fabs, making an angle of 107 degrees with the Fab dyad. The angle between long axes of the Fabs was 115 degrees, the most acute angle yet observed, yielding a distorted Y shaped molecule. This is in contrast to the distorted T shape of the only other intact IgG (2a) whose complete structure is known. Primary lattice interactions arise through formation of VH antiparallel beta ribbons whose strands are contributed by pseudo dyad related H2, and by L3 hypervariable loops from neighboring molecules. While one CH2 domain was mobile, Fabs and three domains of the Fc were well defined, as were hinge polypeptides connecting Fabs to the Fc, and the covalently attached oligosaccharides. Direct interactions are observed between hinge polypeptides, the glycosylated loop of one CH2 domain, and the oligosaccharide. Lattice interactions clearly influence, perhaps even determine the overall conformation of the antibody observed in this crystal. Comparison of this IgG1 with previously determined intact antibody structures extends the conformational range arising from segmental flexibility.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Sequences of proteins of immunological interest
(1984) · Analytical Biochemistry · doi:10.1016/0003-2697(84)90805-4 · Cited by 3,363
Deisenhofer, J. (1981) · PubMed · Cited by 1,422
Deisenhofer, J. (1981) · Biochemistry · doi:10.1021/bi00512a001 · Cited by 1,333
SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules
Evans, S. V. (1993) · Journal of Molecular Graphics · doi:10.1016/0263-7855(93)87009-t · Cited by 1,279
Three-dimensional structure of an antibody-antigen complex.
Sheriff, S., Silverton, E. W., Padlan, E. A., Cohen, G. H., Smith-Gill, S. J., Finzel, B. C., & Davies, D. R. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.22.8075 · Cited by 607
Phosphocholine binding immunoglobulin Fab McPC603
Satow, Y., Cohen, G. H., Padlan, E. A., & Davies, D. R. (1986) · Journal of Molecular Biology · doi:10.1016/0022-2836(86)90245-7 · Cited by 568
Marquart, M., Deisenhofer, J., Huber, R., & Palm, W. (1980) · Journal of Molecular Biology · doi:10.1016/0022-2836(80)90252-1 · Cited by 457
Refined Structure of an Intact IgG2a Monoclonal Antibody,
Harris, L. J., Larson, S. B., Hasel, K. W., & McPherson, A. (1997) · Biochemistry · doi:10.1021/bi962514+ · Cited by 451
Self-citationThree-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
Extension of molecular replacement: a new search strategy based on Patterson correlation refinement
Brünger, A. T. (1990) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767389009633 · Cited by 311
Cited by
Shields, R. L., Lai, J., Keck, R., O'Connell, L. Y., Hong, K., Meng, Y. G., Weikert, S. H. A., & Presta, L. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202069200 · Cited by 1,835
Shinkawa, T., Nakamura, K., Yamane, N., Shoji-Hosaka, E., Kanda, Y., Sakurada, M., Uchida, K., Anazawa, H., Satoh, M., Yamasaki, M., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210665200 · Cited by 1,413
Shields, R. L., Namenuk, A. K., Hong, K., Meng, Y. G., Rae, J., Briggs, J., Xie, D., Lai, J., Stadlen, A., Li, B., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009483200 · Cited by 1,161
Barnes, C. O., West, A. P., Huey-Tubman, K. E., Hoffmann, M. A. G., Sharaf, N. G., Hoffman, P. R., Koranda, N., Gristick, H. B., Gaebler, C., Muecksch, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.025 · Cited by 795
Kanda, Y., Yamada, T., Mori, K., Okazaki, A., Inoue, M., Kitajima-Miyama, K., Kuni-Kamochi, R., Nakano, R., Yano, K., Kakita, S., et al. (2007) · Glycobiology · doi:10.1093/glycob/cwl057 · Cited by 372
Metadata
- Authors
- Harris, L. J., Skaletsky, E., & McPherson, A.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1998-02
- Volume
- 275
- Issue
- 5
- Pages
- 861-872
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2009671611
- Cited by
- 440
- References
- 17
- Type
- book review
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Crystallographic structure of an intact IgG1 monoclonal antibody 1 1Edited by I. A. Wilson. https://app.cochat.ai/papers/10.1006/jmbi.1997.1508
- The paper
- Harris, L. J., Skaletsky, E., & McPherson, A. (1998). Crystallographic structure of an intact IgG1 monoclonal antibody 1 1Edited by I. A. Wilson. Journal of Molecular Biology. https://doi.org/10.1006/jmbi.1997.1508
Data sources
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.
