Journal article
Prostaglandin H synthase
Current opinion in structural biology, v 4(4), pp 529-535
1994
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The prostaglandin H synthase structure reveals that the enzyme has a fold similar to those of other heme peroxidases, but differing in that a second active site has evolved within this fold which catalyzes the cyclooxygenase reaction. The protein has also acquired two additional domains: a membrane-binding motif that lacks transmembrane segments, mediating attachment to the membrane via helices that lie parallel to the membrane, and an epidermal growth factor-like module found just before the membrane-binding motif. The epidermal growth factor-like module is located in the dimer interface.
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Details
- Title
- Prostaglandin H synthase
- Creators
- R.Michael Garavito - University of ChicagoDaniel Picot - University of ChicagoPatrick J. Loll - University of Chicago
- Publication Details
- Current opinion in structural biology, v 4(4), pp 529-535
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:A1994QB25600008
- Scopus ID
- 2-s2.0-0028071559
- Other Identifier
- 991019295015804721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology
- Cell Biology