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| THE X-RAY CRYSTAL-STRUCTURE OF THE MEMBRANE-PROTEIN PROSTAGLANDIN-H(2) SYNTHASE-1 |
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| Author(s): PICOT D, LOLL PJ, GARAVITO RM |
| Source: NATURE Volume: 367 Issue: 6460 Pages: 243-249 Published: JAN 20 1994 |
| Times Cited: 850 References: 49 |
| Abstract: The three-dimensional structure of prostaglandin H-2 synthase-1, an integral membrane Protein, has been determined at 3.5 angstrom resolution by X-ray crystallography. This bifunctional enzyme comprises three independent folding units: an epidermal growth factor domain, a membrane-binding motif and an enzymatic domain. Two adjacent but spatially distinct active sites were found for its haem-dependent peroxidase and cyclooxygenase activities. The cyclooxygenase active site is created by a long, hydrophobic channel that is the site of non-steroidal anti-inflammatory drug binding. The conformation of the membrane-binding motif strongly suggests that the enzyme integrates into only one leaflet of the lipid bilayer and is thus a monotopic membrane protein. |
| Document Type: Article |
| Language: English |
Addresses:
1. UNIV CHICAGO, DEPT BIOCHEM & MOLEC BIOL, 920 E 58TH ST, CHICAGO, IL 60637 USA |
| Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: MR494 |
| ISSN: 0028-0836 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |