PROSTAGLANDIN-H SYNTHASE - IMPLICATIONS FOR MEMBRANE

被引：57

作者：

PICOT, D ^{[1
]}

GARAVITO, RM ^{[1
]}

机构：

[1] UNIV CHICAGO,DEPT BIOCHEM & MOLEC BIOL,CHICAGO,IL 60637

来源：

FEBS LETTERS | 1994年 / 346卷 / 01期

关键词：

MEMBRANE PROTEIN STRUCTURE; CYCLOOXYGENASE; PEROXIDASE; X-RAY STRUCTURE;

D O I：

10.1016/0014-5793(94)00314-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The 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 epidermial 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.

引用

页码：21 / 25

页数：5

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