Co-evolving motions at protein-protein interfaces of two-component signaling systems identified by covariance analysis.
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ABSTRACT:
SUBMITTER: Szurmant H
PROVIDER: S-EPMC2830073 | biostudies-literature | 2008 Jul
REPOSITORIES: biostudies-literature
Publications
Co-evolving motions at protein-protein interfaces of two-component signaling systems identified by covariance analysis.
Szurmant Hendrik H Bobay Benjamin G BG White Robert A RA Sullivan Daniel M DM Thompson Richele J RJ Hwa Terence T Hoch James A JA Cavanagh John J
Biochemistry 20080628 30
Short-lived protein interactions determine signal transduction specificity among genetically amplified, structurally identical two-component signaling systems. Interacting protein pairs evolve recognition precision by varying residues at specific positions in the interaction surface consistent with constraints of charge, size, and chemical properties. Such positions can be detected by covariance analyses of two-component protein databases. Here, covariance is shown to identify a cluster of co-ev ...[more]
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