Structures of fluoro, amino, and thiol inhibitors bound to the [Fe 4S4] protein IspH

Span I, Wang K, Wang W, Jauch J, Eisenreich W, Bacher A, Oldfield E, Groll M (2013)


Publication Type: Journal article

Publication year: 2013

Journal

Book Volume: 52

Pages Range: 2118-2121

Journal Issue: 7

DOI: 10.1002/anie.201208469

Abstract

The iron-sulfur protein IspH catalyzes a key step in isoprenoid biosynthesis in bacteria and malaria parasites. Crystal structures of IspH complexed with three substrate analogues reveal their mode of binding and suggest new routes to inhibitor design. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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APA:

Span, I., Wang, K., Wang, W., Jauch, J., Eisenreich, W., Bacher, A.,... Groll, M. (2013). Structures of fluoro, amino, and thiol inhibitors bound to the [Fe 4S4] protein IspH. Angewandte Chemie International Edition, 52(7), 2118-2121. https://doi.org/10.1002/anie.201208469

MLA:

Span, Ingrid, et al. "Structures of fluoro, amino, and thiol inhibitors bound to the [Fe 4S4] protein IspH." Angewandte Chemie International Edition 52.7 (2013): 2118-2121.

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