Structure, function, and evolution of transient and obligate protein–protein interactions Link
Recent analyses of high-throughput protein interaction data coupled with
large-scale investigations of evolutionary properties
of interaction networks have left some unanswered
questions. To what extent do protein interactions act as constraints
during
evolution of the protein sequence? How does the
type of interaction, specifically transient or obligate, play into these
constraints?
Are the mutations in the binding site of an
interacting protein correlated with mutations in the binding site of its
partner?
We address these and other questions by relying on a
carefully curated dataset of protein complex structures. Results point
to the importance of distinguishing between
transient and obligate interactions. We conclude that residues in the
interfaces
of obligate complexes tend to evolve at a
relatively slower rate, allowing them to coevolve with their interacting
partners.
In contrast, the plasticity inherent in transient
interactions leads to an increased rate of substitution for the
interface
residues and leaves little or no evidence of
correlated mutations across the interface.
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