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Prostaglandin H synthase: implications for membrane structure Picot D; Garavito RMFEBS Lett 1994[Jun]; 346 (1): 21-5The crystal structure of the membrane protein prostaglandin H synthase (PGHS) provides strong evidence for the existence of monotopic membrane proteins: PGHS seems to interact with the membrane via a motif of amphipathic helices positioned parallel to the plane of the membrane. The orientation of this unique membrane binding motif is fixed in space by an epidermal growth factor(EGF)-like module on its amino-terminal end and by the catalytic domain at its carboxy-terminal end. The catalytic domain of PGHS has a high structural homology to other mammalian heme peroxidases.|Amino Acid Sequence[MESH]|Crystallization[MESH]|Macromolecular Substances[MESH]|Membrane Proteins/*chemistry[MESH]|Models, Molecular[MESH]|Molecular Sequence Data[MESH]|Prostaglandin-Endoperoxide Synthases/*chemistry[MESH]|Protein Structure, Secondary[MESH] |
