Picot D, Garavito R M
Department of Biochemistry and Molecular Biology, University of Chicago, IL 60637.
FEBS Lett. 1994 Jun 6;346(1):21-5. doi: 10.1016/0014-5793(94)00314-9.
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 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.
膜蛋白前列腺素H合酶(PGHS)的晶体结构为单一位点膜蛋白的存在提供了有力证据:PGHS似乎通过与膜平面平行定位的两亲性螺旋基序与膜相互作用。这个独特的膜结合基序的方向在空间上由其氨基末端的表皮生长因子(EGF)样模块和羧基末端的催化结构域固定。PGHS的催化结构域与其他哺乳动物血红素过氧化物酶具有高度的结构同源性。