Highly discriminating protein-protein interaction specificities in the context of a conserved binding energy hotspot.

Journal article

We explore the thermodynamic basis for high affinity binding and specificity in conserved protein complexes using colicin endonuclease-immunity protein complexes as our model system. We investigated the ability of each colicin-specific immunity protein (Im2, Im7, Im8 and Im9) to bind the endonuclease (DNase) domains of colicins E2, E7 and E8 in vitro and compared these to the previously studied colicin E9. We find that high affinity binding (Kd < or = 10(-14) M) is a common feature of cogn...

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Authors: Li, W; Keeble, A; Giffard, C; James, R; Moore, G

• Journal: Journal of molecular biology
• Volume: 337
• Issue: 3
• Pages: 743-759
• Publication date: 2004-03-01
• DOI: 10.1016/j.jmb.2004.02.005
• EISSN: 1089-8638
• ISSN: 0022-2836
• Language: English
• Keywords: Colicins; Substrate Specificity; Conserved Sequence; Kinetics; Endonucleases; Protein Binding; Bacterial Proteins; Thermodynamics; Binding Sites