Protein clefts in molecular recognition and function.

@article{Laskowski1996ProteinCI,
  title={Protein clefts in molecular recognition and function.},
  author={Roman A. Laskowski and Nicholas M. Luscombe and Mark B. Swindells and Janet M. Thornton},
  journal={Protein science : a publication of the Protein Society},
  year={1996},
  volume={5 12},
  pages={2438-52}
}
One of the primary factors determining how proteins interact with other molecules is the size of clefts in the protein's surface. In enzymes, for example, the active site is often characterized by a particularly large and deep cleft, while interactions between the molecules of a protein dimer tend to involve approximately planar surfaces. Here we present an analysis of how cleft volumes in proteins relate to their molecular interactions and functions. Three separate datasets are used… CONTINUE READING

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A procedure for detecting structural domains in proteins

  • Swindells MB.
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  • 1995
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