Protein-protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfaces.

@article{Ma2003ProteinproteinIS,
  title={Protein-protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfaces.},
  author={Buyong Ma and Tal Elkayam and Haim J. Wolfson and Ruth Nussinov},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2003},
  volume={100 10},
  pages={5772-7}
}
Polar residue hot spots have been observed at protein-protein binding sites. Here we show that hot spots occur predominantly at the interfaces of macromolecular complexes, distinguishing binding sites from the remainder of the surface. Consequently, hot spots can be used to define binding epitopes. We further show a correspondence between energy hot spots and structurally conserved residues. The number of structurally conserved residues, particularly of high ranking energy hot spots, increases… CONTINUE READING
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Structure (London) 8, R137–R142

E. J. Sundberg, R. A. Mariuzza
2000

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