Cation-π interactions in structural biology
- Creators
- Gallivan, Justin P.
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Dougherty, Dennis A.
Abstract
Cation-pi interactions in protein structures are identified and evaluated by using an energy-based criterion for selecting significant sidechain pairs. Cation-pi interactions are found to be common among structures in the Protein Data Bank, and it is clearly demonstrated that, when a cationic sidechain (Lys or Arg) is near an aromatic sidechain (Phe, Tyr, or Trp), the geometry is biased toward one that would experience a favorable cation-pi interaction. The sidechain of Arg is more likely than that of Lys to be in a cation-pi interaction. Among the aromatics, a strong bias toward Trp is clear, such that over one-fourth of all tryptophans in the data bank experience an energetically significant cation-pi interaction.
Additional Information
© 1999 by the National Academy of Sciences. Communicated by Robert Grubbs, California Institute of Technology, Pasadena, CA, June 16, 1999 (received for review April 13, 1999). We thank Dr. Scott Silverman for fruitful discussions. J.P.G. thanks the Eastman Kodak Corporation for generous fellowship support. This work was supported by the National Institutes of Health (Grant NS34407). The CAPTURE program can be obtained from the authors by e-mail request. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.Attached Files
Published - GALpnas99.pdf
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Additional details
- PMCID
- PMC22230
- Eprint ID
- 920
- Resolver ID
- CaltechAUTHORS:GALpnas99
- Eastman Kodak Company
- NIH
- NS34407
- Created
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2005-11-08Created from EPrint's datestamp field
- Updated
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2021-11-08Created from EPrint's last_modified field