The statistical significance of selected sense-antisense peptide interactions

Copyright © 2012 Wiley Periodicals, Inc.

Bibliographische Detailangaben
Veröffentlicht in:Journal of computational chemistry. - 1984. - 33(2012), 16 vom: 15. Juni, Seite 1440-7
1. Verfasser: Illingworth, Christopher J R (VerfasserIn)
Weitere Verfasser: Chintipalli, Sree V, Serapian, Stefano A, Miller, Andrew D, Veverka, Vaclav, Carr, Mark D, Reynolds, Christopher A
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2012
Zugriff auf das übergeordnete Werk:Journal of computational chemistry
Schlagworte:Journal Article IL‐1F2 MI pairs antisense peptides complementary residue pairs docking glide molecular interactions protein peptide interaction protein–protein interactions mehr... sense peptides Codon Interleukin-1 Oligonucleotides, Antisense Protein Isoforms
Beschreibung
Zusammenfassung:Copyright © 2012 Wiley Periodicals, Inc.
Sense and antisense peptides, encoded by sense and corresponding antisense DNA strands, are capable of specific interactions that could be a driving force to mediate protein-protein or protein-peptide binding associations. The complementary residue hypothesis suggests that these interactions are founded upon the sum of pairwise interactions between amino acids encoded by corresponding sense and antisense codons. Despite many successful experimental results obtained with the hypothesis, however, the physicochemical basis for these interactions is poorly understood. We examined the potential of the hypothesis for general identification of protein-protein interaction sites, and the possible role of the hypothesis in determining folding in a broad set of protein structures. In addition, we performed a structural study to investigate the binding of a complementary peptide to IL-1F2. Our results suggest that complementary residue pairs are no more frequent or conserved than average in protein-protein interfaces, and are statistically under-represented amongst contacting residue pairs in folded protein structures. Although our structural results matched experimental observations of binding between the peptide and IL-1F2, complementary residue interactions do not appear to be dominant in the bound structure. Overall, our data do not allow us to conclude that the complementary residue hypothesis accounts for specific sense-antisense peptide interactions
Beschreibung:Date Completed 06.10.2015
Date Revised 29.01.2022
published: Print-Electronic
Citation Status MEDLINE
ISSN:1096-987X
DOI:10.1002/jcc.22977