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Nucleic Acids Research Advance Access originally published online on June 12, 2007
Nucleic Acids Research 2007 35(Web Server issue):W398-W402; doi:10.1093/nar/gkm351
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Nucleic Acids Research, 2007, Vol. 35, No. suppl_2 W398-W402
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Articles

eF-seek: prediction of the functional sites of proteins by searching for similar electrostatic potential and molecular surface shape

Kengo Kinoshita1,2,*, Yoichi Murakami3 and Haruki Nakamura3

1Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minatoku, Tokyo, 108-8639, Japan, 2Structure and Function of Biomolecules, SORST, Japan Science and Technology Corporation, 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan and 3Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871, Japan

*To whom correspondence should be addressed. Tel: +81-3-5449-5131; Fax: +81 3 5449-5133; Email: kino{at}ims.u-tokyo.ac.jp

Received January 30, 2007. Revised April 22, 2007. Accepted April 23, 2007.

We have developed a method to predict ligand-binding sites in a new protein structure by searching for similar binding sites in the Protein Data Bank (PDB). The similarities are measured according to the shapes of the molecular surfaces and their electrostatic potentials. A new web server, eF-seek, provides an interface to our search method. It simply requires a coordinate file in the PDB format, and generates a prediction result as a virtual complex structure, with the putative ligands in a PDB format file as the output. In addition, the predicted interacting interface is displayed to facilitate the examination of the virtual complex structure on our own applet viewer with the web browser (URL: http://eF-site.hgc.jp/eF-seek).


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 Brief BioinformHome page
D. M. Standley, A. R. Kinjo, K. Kinoshita, and H. Nakamura
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[Abstract] [Full Text] [PDF]


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