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Coupled Folding and Binding with α-Helix-Forming Molecular Recognition Elements
Abstract
Many protein-protein and protein-nucleic acid interactions involve coupled folding and binding of at least one of the partners. Here, we propose a protein structural element or feature that mediates the binding events of initially disordered regions. This element consists of a short region that undergoes coupled binding and folding within a longer region of disorder. We call these features "molecular recognition elements" (MoREs). Examples of MoREs bound to their partners can be found in the alpha-helix, beta-strand, polyproline II helix, or irregular secondary structure conformations, and in various mixtures of the four structural forms. Here we describe an algorithm that identifies regions having propensities to become alpha-helix-forming molecular recognition elements (alpha-MoREs) based on a discriminant function that indicates such regions while giving a low false-positive error rate on a large collection of structured proteins. Application of this algorithm to databases of genomics and functionally annotated proteins indicates that alpha-MoREs are likely to play important roles protein-protein interactions involved in signaling events.
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Metadata
- Authors
- Oldfield, C. J., Cheng, Y., Cortese, M. S., Romero, P., Uversky, V. N., & Dunker, A. K.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2005-08-24
- Volume
- 44
- Issue
- 37
- Pages
- 12454-12470
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2027035874
- Cited by
- 630
- References
- 11
- FWCI
- 7.84
- Type
- journal article
- Language
- en
- Open access
- closed
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