The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Exploiting the Basis of Proline Recognition by SH3 and WW Domains: Design of N-Substituted Inhibitors
Abstract
Src homology 3 (SH3) and WW protein interaction domains bind specific proline-rich sequences. However, instead of recognizing critical prolines on the basis of side chain shape or rigidity, these domains broadly accepted amide N-substituted residues. Proline is apparently specifically selected in vivo, despite low complementarity, because it is the only endogenous N-substituted amino acid. This discriminatory mechanism explains how these domains achieve specific but low-affinity recognition, a property that is necessary for transient signaling interactions. The mechanism can be exploited: screening a series of ligands in which key prolines were replaced by nonnatural N-substituted residues yielded a ligand that selectively bound the Grb2 SH3 domain with 100 times greater affinity.
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Metadata
- Authors
- Nguyen, J. T., Turck, C. W., Cohen, F. E., Zuckermann, R. N., & Lim, W. A.
- Venue
- Science
- Published
- 1998-12-11
- Volume
- 282
- Issue
- 5396
- Pages
- 2088-2092
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1971447541
- Cited by
- 314
- References
- 27
- FWCI
- 7.65
- Type
- journal article
- Language
- en
- Open access
- closed
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- Nguyen, J. T., Turck, C. W., Cohen, F. E., Zuckermann, R. N., & Lim, W. A. (1998). Exploiting the Basis of Proline Recognition by SH3 and WW Domains: Design of N-Substituted Inhibitors. Science. https://doi.org/10.1126/science.282.5396.2088
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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