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Science 17 December 1999:
Vol. 286. no. 5448, pp. 2345 - 2348
DOI: 10.1126/science.286.5448.2345
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Reports

Evolution of Shape Complementarity and Catalytic Efficiency from a Primordial Antibody Template

Jian Xu, 1* Qiaolin Deng, 2 Jiangang Chen, 2 Kendall N. Houk, 2 Johannes Bartek, 3 Donald Hilvert, 3 Ian A. Wilson 1

The crystal structure of an efficient Diels-Alder antibody catalyst at 1.9 angstrom resolution reveals almost perfect shape complementarity with its transition state analog. Comparison with highly related progesterone and Diels-Alderase antibodies that arose from the same primordial germ line template shows the relatively subtle mutational steps that were able to evolve both structural complementarity and catalytic efficiency.

1 Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
2 Department of Chemistry and Biochemistry, University of California, Los Angeles, 405 Hilgard Avenue, Los Angeles, CA 90095-1569, USA.
3 Laboratory of Organic Chemistry, Swiss Federal Institute of Technology (ETH), Universitätstrasse 16, CH-8092 Zurich, Switzerland.
*   Present address: Molecular Simulations Inc., 9685 Scranton Road, San Diego, CA 92121, USA.

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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J. Biol. Chem. 275, 38393-38401
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Science. ISSN 0036-8075 (print), 1095-9203 (online)