Peptides mediating interaction networks: new leads at last
V Neduva, RB Russell - Current opinion in biotechnology, 2006 - Elsevier
V Neduva, RB Russell
Current opinion in biotechnology, 2006•ElsevierA growing number of protein interactions are found to be mediated by a large globular
region in one protein binding to a comparatively short, peptide stretch in another. Regions
that bind a common protein often show a similar sequence pattern or linear motif that
mediates the binding. The past year has seen reports of new techniques that can uncover
these motifs directly from interaction data. These studies have suggested that the fraction of
interactions mediated by these regions is greater than previously anticipated. Concurrently …
region in one protein binding to a comparatively short, peptide stretch in another. Regions
that bind a common protein often show a similar sequence pattern or linear motif that
mediates the binding. The past year has seen reports of new techniques that can uncover
these motifs directly from interaction data. These studies have suggested that the fraction of
interactions mediated by these regions is greater than previously anticipated. Concurrently …
A growing number of protein interactions are found to be mediated by a large globular region in one protein binding to a comparatively short, peptide stretch in another. Regions that bind a common protein often show a similar sequence pattern or linear motif that mediates the binding. The past year has seen reports of new techniques that can uncover these motifs directly from interaction data. These studies have suggested that the fraction of interactions mediated by these regions is greater than previously anticipated. Concurrently, other work has demonstrated that it is possible to target these interactions using small molecules. Together these developments hold great promise for future efforts to target chemically precise details of complex systems.
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