The DOI matches its Crossref record.
The structure of protein-protein recognition sites.
Open accessAbstract
The ability of certain proteins to form specific stable complexes is fundamental to biological existence. The structures of some 15 protease-inhibitor complexes (l-19) and 4 anti-body-protein antigen complexes (20-26) have been determined by x-ray crystallography, and we review the informa-tion that they provide on the structural basis of protein- protein recognition, We describe first the general features of the recognition sites. We then discuss whether recognition sites are regions of high mobility, the nature of the conformational changes that occur on the association of proteins, and the implications of these structural results for the kinetics and thermodynamics of association. view is largely confirmed structures
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
Principles of protein-protein interactions
Jones, S., & Thornton, J. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.13 · Cited by 2,684
The Ras-RasGAP Complex: Structural Basis for GTPase Activation and Its Loss in Oncogenic Ras Mutants
Scheffzek, K., Ahmadian, M. R., Kabsch, W., Wiesmüller, L., Lautwein, A., Schmitz, F., & Wittinghofer, A. (1997) · Science · doi:10.1126/science.277.5324.333 · Cited by 1,543
Principles of docking: An overview of search algorithms and a guide to scoring functions
Halperin, I., Ma, B., Wolfson, H., & Nussinov, R. (2002) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10115 · Cited by 1,294
Diversity in the CDR3 Region of VH Is Sufficient for Most Antibody Specificities
Xu, J. L., & Davis, M. M. (2000) · Immunity · doi:10.1016/s1074-7613(00)00006-6 · Cited by 779
Hot spots—A review of the protein–protein interface determinant amino‐acid residues
Moreira, I. S., Fernandes, P. A., & Ramos, M. J. (2007) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.21396 · Cited by 760
Crystal Structure of Human Cyclophilin A Bound to the Amino-Terminal Domain of HIV-1 Capsid
Gamble, T. R., Vajdos, F. F., Yoo, S., Worthylake, D. K., Houseweart, M., Sundquist, W. I., & Hill, C. P. (1996) · Cell · doi:10.1016/s0092-8674(00)81823-1 · Cited by 706
“Our face area is smaller than most stable protein–protein interfaces (Janin and Chothia, 1990), consistent with theCA151/CypA structure does not explain this observation, however, since each CypA makes specific contacts to modest dissociation constant of the CA/CypA complex.”
BackgroundThe structural basis of antibody–antigen recognition
Sela-Culang, I., Kunik, V., & Ofran, Y. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00302 · Cited by 530
Keskin, O., Ma, B., & Nussinov, R. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.10.077 · Cited by 519
Structural biology of bacterial iron uptake
Krewulak, K. D., & Vogel, H. J. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.07.026 · Cited by 512
Selectivity determinants of GPCR–G-protein binding
Flock, T., Hauser, A. S., Lund, N., Gloriam, D. E., Balaji, S., & Babu, M. M. (2017) · Nature · doi:10.1038/nature22070 · Cited by 384
Ni, D., Lu, S., & Zhang, J. (2019) · Medicinal Research Reviews · doi:10.1002/med.21585 · Cited by 116
The role of protonation states in ligand-receptor recognition and binding.
Petukh, M., Stefl, S., & Alexov, E. (2013) · Current Pharmaceutical Design · doi:10.2174/1381612811319230004 · Cited by 101
Kunik, V., & Ofran, Y. (2013) · Protein Engineering Design and Selection · doi:10.1093/protein/gzt027 · Cited by 96
Brown, A. J., Snapkov, I., Akbar, R., Pavlović, M., Miho, E., Sandve, G. K., & Greiff, V. (2019) · Molecular Systems Design & Engineering · doi:10.1039/c9me00071b · Cited by 59
Are there physicochemical differences between allosteric and competitive ligands?
Smith, R. D., Lu, J., & Carlson, H. A. (2017) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1005813 · Cited by 27
Bolz, S. N., Schake, P., Stitz, C., & Schroeder, M. (2025) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2025.2557599 · Cited by 7
Metadata
- Authors
- Janin, J., & Chothia, C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1990-09
- Volume
- 265
- Issue
- 27
- Pages
- 16027-16030
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1526151739
- Cited by
- 819
- References
- 0
- FWCI
- 11.75
- 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
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.