The DOI matches its Crossref record; 112 of the 112 references it cites were found in a registry or an index.
Recognition of Proline‐Rich Motifs by Protein–Protein‐Interaction Domains
Abstract
Protein–protein interactions are essential in every aspect of cellular activity. Multiprotein complexes form and dissociate constantly in a specifically tuned manner, often by conserved mechanisms. Protein domains that bind proline‐rich motifs (PRMs) are frequently involved in signaling events. The unique properties of proline provide a mechanism for highly discriminatory recognition without requiring high affinities. We present herein a detailed, quantitative assessment of the structural features that define the interfaces between PRM‐binding domains and their target PRMs, and investigate the specificity of PRM recognition. Together with the analysis of peptide‐library screens, this approach has allowed the identification of several highly conserved key interactions found in all complexes of PRM‐binding domains. The inhibition of protein–protein interactions by using small‐molecule agents is very challenging. Therefore, it is important to first pinpoint the critical interactions that must be considered in the design of inhibitors of PRM‐binding domains.
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Cites
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Cited by
Loss of Function of a Proline-Containing Protein Confers Durable Disease Resistance in Rice
Fukuoka, S., Saka, N., Koga, H., Ono, K., Shimizu, T., Ebana, K., Hayashi, N., Takahashi, A., Hirochika, H., Okuno, K., et al. (2009) · Science · doi:10.1126/science.1175550 · Cited by 678
Amniai, L., Barbier, P., Sillen, A., Wieruszeski, J.-M., Peyrot, V., Lippens, G., & Landrieu, I. (2009) · The FASEB Journal · doi:10.1096/fj.08-121590 · Cited by 105
ATAD3 proteins: brokers of a mitochondria–endoplasmic reticulum connection in mammalian cells
Baudier, J. (2018) · Biological Reviews · doi:10.1111/brv.12373 · Cited by 99
Lalevee, S., Bour, G., Quinternet, M., Samarut, E., Kessler, P., Vitorino, M., Bruck, N., Delsuc, M., Vonesch, J., Kieffer, B., et al. (2010) · The FASEB Journal · doi:10.1096/fj.10-160572 · Cited by 32
Singer, A., Ramos, A., & Keating, A. E. (2024) · Protein Science · doi:10.1002/pro.5094 · Cited by 6
Metadata
- Authors
- Ball, L. J., Kühne, R., Schneider‐Mergener, J., & Oschkinat, H.
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2005-05-03
- Volume
- 44
- Issue
- 19
- Pages
- 2852-2869
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- OpenAlex
- W2021226373
- Cited by
- 254
- References
- 112
- FWCI
- 4.26
- Type
- journal article
- Language
- en
- Open access
- closed
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