The DOI matches its Crossref record.
Crystallographic refinement of the three-dimensional structure of the FabD1.3-lysozyme complex at 2.5-A resolution
Open accessAbstract
The three-dimensional crystal structure of the complex between the Fab from the monoclonal anti-lysozyme antibody D1.3 and the antigen, hen egg white lysozyme, has been refined by crystallographic techniques using x-ray intensity data to 2.5-A resolution. The antibody contacts the antigen with residues from all its complementarity determining regions. Antigen residues 18-27 and 117-125 form a discontinuous antigenic determinant making hydrogen bonds and van der Waals interactions with the antibody. Water molecules at or near the antigen-antibody interface mediate some contacts between antigen and antibody. The fine specificity of antibody D1.3, which does not bind (K alpha less than 10(5) M-1) avian lysozymes where Gln121 in the amino acid sequence is occupied by His, can be explained on the basis of the refined model.
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
Cited by
"Diabodies": small bivalent and bispecific antibody fragments.
Holliger, P., Prospero, T., & Winter, G. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.14.6444 · Cited by 874
Gabb, H. A., Jackson, R. M., & Sternberg, M. J. E. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1203 · Cited by 817
Standard conformations for the canonical structures of immunoglobulins 1 1Edited by I. A. Wilson
Al-Lazikani, B., Lesk, A. M., & Chothia, C. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1354 · Cited by 706
Evaluation and improvement of multiple sequence methods for protein secondary structure prediction
Cuff, J. A., & Barton, G. J. (1999) · Proteins: Structure, Function, and Genetics · doi:10.1002/(sici)1097-0134(19990301)34:4<508::aid-prot10>3.0.co;2-4 · Cited by 667
A role for surface hydrophobicity in protein‐protein recognition
Young, L., Jernigan, R. L., & Covell, D. G. (1994) · Protein Science · doi:10.1002/pro.5560030501 · Cited by 391
Metadata
- Authors
- Fischmann, T. O., Bentley, G. A., Bhat, T. N., Boulot, G., Mariuzza, R. A., Phillips, S. E., Tello, D., & Poljak, R. J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1991-07
- Volume
- 266
- Issue
- 20
- Pages
- 12915-12920
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1858317139
- Cited by
- 174
- References
- 0
- FWCI
- 15.78
- Type
- journal article
- Language
- en
- Open access
- hybrid
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 refinement of the three-dimensional structure of the FabD1.3-lysozyme complex at 2.5-A resolution. https://app.cochat.ai/papers/10.1016/s0021-9258(18)98782-x
- The paper
- Fischmann, T. O., Bentley, G. A., Bhat, T. N., Boulot, G., Mariuzza, R. A., Phillips, S. E., Tello, D., & Poljak, R. J. (1991). Crystallographic refinement of the three-dimensional structure of the FabD1.3-lysozyme complex at 2.5-A resolution. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)98782-x
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.