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. 1994 May;3(5):717-29.
doi: 10.1002/pro.5560030501.

A role for surface hydrophobicity in protein-protein recognition

L Young  1 , R L Jernigan, D G Covell
Affiliations

A role for surface hydrophobicity in protein-protein recognition

L Young et al. Protein Sci. 1994 May.

Abstract

The role of hydrophobicity as a determinant of protein-protein interactions is examined. Surfaces of apo-protein targets comprising 9 classes of enzymes, 7 antibody fragments, hirudin, growth hormone, and retinol-binding protein, and their associated ligands with available X-ray structures for their complexed forms, are scanned to determine clusters of surface-accessible amino acids. Clusters of surface residues are ranked on the basis of the hydrophobicity of their constituent amino acids. The results indicate that the location of the co-crystallized ligand is commonly found to correspond with one of the strongest hydrophobic clusters on the surface of the target molecule. In 25 of 38 cases, the correspondence is exact, with the position of the most hydrophobic cluster coinciding with more than one-third of the surface buried by the bound ligand. The remaining 13 cases demonstrate this correspondence within the top 6 hydrophobic clusters. These results suggest that surface hydrophobicity can be used to identify regions of a protein's surface most likely to interact with a binding ligand. This fast and simple procedure may be useful for identifying small sets of well-defined loci for possible ligand attachment.

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References

    1. Nature. 1992 Nov 26;360(6402):364-6 - PubMed
    1. Nucleic Acids Res. 1992 May 11;20 Suppl:2013-8 - PubMed
    1. J Biol Chem. 1991 Jul 15;266(20):12915-20 - PubMed
    1. Proteins. 1991;11(4):281-96 - PubMed
    1. Science. 1990 Nov 23;250(4984):1121-5 - PubMed

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