PerspectiveComputational Biology

Mapping global protein contacts

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Science  12 Jul 2019:
Vol. 365, Issue 6449, pp. 120-121
DOI: 10.1126/science.aay1440

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Summary

The divergence of orthologous protein sequences across evolutionary lineages can be used to pinpoint possible contacts at specific amino acids by exploiting the tendency for compensating mutations to coevolve at interacting positions within proteins (1). This coevolutionary approach has galvanized the vast improvement in protein-structure prediction over the past two decades (2). It has also been used to locate contact points between pairs of interacting proteins (3), which can serve as distance restraints for high-quality models of multiprotein complexes by structural docking (4). On page 185 of this issue, Cong et al. (5) use this method to explore potential interactions among all Escherichia coli and Mycobacterium tuberculosis proteins and thereby enhance knowledge of bacterial protein interaction networks (interactomes).