The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Hinge-bending in L-arabinose-binding protein. The “Venus's-flytrap” model.
Open accessAbstract
Theoretical conformational energy calculations show that large changes in the width of the binding-site cleft in the L-arabinose-binding protein involve only modest changes in the protein internal energy. Solvation energy changes associated with such variations of the cleft width and with protein-ligand interactions are estimated to be significantly larger than the internal energy changes. These results indicate that the binding-site cleft is open in the unliganded protein and is induced to close upon ligation. This picture is consistent with experimental data on the structure and binding kinetics of the L-arabinose-binding protein and provides a physical framework for interpreting such data.
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Citations
Cites
AREAS, VOLUMES, PACKING, AND PROTEIN STRUCTURE
Richards, F. M. (1977) · Annual Review of Biophysics and Bioengineering · doi:10.1146/annurev.bb.06.060177.001055 · Cited by 2,661
Page, M. I., & Jencks, W. P. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.8.1678 · Cited by 1,014
The hinge-bending mode in lysozyme
MCCAMMON, J. A., GELIN, B. R., KARPLUS, M., & WOLYNES, P. G. (1976) · Nature · doi:10.1038/262325a0 · Cited by 379
Self-citationPicosecond dynamics of tyrosine side chains in proteins
McCammon, J. A., Wolynes, P. G., & Karplus, M. (1979) · Biochemistry · doi:10.1021/bi00573a001 · Cited by 336
Self-citationBerry, R. S. (1980) · Cited by 216
Gated binding of ligands to proteins
McCammon, J. A., & Northrup, S. H. (1981) · Nature · doi:10.1038/293316a0 · Cited by 149
Self-citationThe radius of gyration of L-arabinose-binding protein decreases upon binding of ligand.
Newcomer, M. E., Lewis, B. A., & Quiocho, F. A. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43030-x · Cited by 115
Self-citationStructure of the l-arabinose-binding protein from Escherichia coli at 2.4 Å resolution
Gilliland, G. L., & Quiocho, F. A. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90392-2 · Cited by 101
Self-citationIntramolecular flexibility in phenylalanine transfer RNA
Harvey, S. C., & McCammon, J. A. (1981) · Nature · doi:10.1038/294286a0 · Cited by 47
Self-citationNewcomer, M. E., Miller, D. M., & Quiocho, F. A. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35976-3 · Cited by 43
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Cited by
ABC Transporters: From Microorganisms to Man
Higgins, C. F. (1992) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.08.110192.000435 · Cited by 3,985
Nakanishi, N., Shneider, N. A., & Axel, R. (1990) · Neuron · doi:10.1016/0896-6273(90)90212-x · Cited by 595
Sharff, A. J., Rodseth, L. E., Spurlino, J. C., & Quiocho, F. A. (1992) · Biochemistry · doi:10.1021/bi00159a003 · Cited by 477
Self-citationSpurlino, J. C., Lu, G.-Y., & Quiocho, F. A. (1992) · Worldwide Protein Data Bank · doi:10.2210/pdb1mbp/pdb · Cited by 458
Self-citationSpurlino, J. C., Lu, G. Y., & Quiocho, F. A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67774-4 · Cited by 455
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Metadata
- Authors
- Mao, B., Pear, M. R., McCammon, J. A., & Quiocho, F. A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1982-02
- Volume
- 257
- Issue
- 3
- Pages
- 1131-1133
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1482516139
- Cited by
- 268
- References
- 11
- FWCI
- 3.44
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Mao, B., Pear, M. R., McCammon, J. A., & Quiocho, F. A. (1982). Hinge-bending in L-arabinose-binding protein. The “Venus's-flytrap” model. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)68161-5
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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.
