Structure and mechanism of intramembrane protease.
Structure and mechanism of intramembrane protease.
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DOI：
10.1016/j.semcdb.2008.11.006
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发表时间：
2009-04
影响因子：
7.3
通讯作者：
Ha Y
中科院分区：
文献类型：
--
作者：
Ha Y
许多功能重要的膜蛋白在其跨膜螺旋内被切割以被激活。这种不寻常的反应是由一组高度专业化和膜结合蛋白酶催化的。在这里，我简要地总结了目前的知识，其结构和机制，重点是菱形家庭。现在已经清楚，菱形蛋白酶不仅可以在跨膜结构域内切割底物，而且可以在溶剂暴露的跨膜区域中切割底物。这种双重特异性似乎是可能的，因为蛋白酶活性位点位于一个浅口袋中，可以通过一个灵活的加帽环的运动直接打开水溶液。狭窄的跨膜区域的蛋白酶表明一种可能的机制，用于访问位于底物跨膜螺旋末端附近的易裂键。类似的原理可以应用于金属蛋白酶家族，其中晶体结构也变得可用。虽然GxGD蛋白酶如何工作仍然不太清楚，但最近的结果表明，早老蛋白似乎也从跨膜螺旋的末端剪切底物。
Many functionally important membrane proteins are cleaved within their transmembrane helices to become activated. This unusual reaction is catalyzed by a group of highly specialized and membrane-bound proteases. Here I briefly summarize current knowledge about their structure and mechanism, with a focus on the rhomboid family. It has now become clear that rhomboid protease can cleave substrates not only within transmembrane domains, but also in the solvent-exposed juxtamembrane region. This dual specificity seems possible because the protease active site is positioned in a shallow pocket that can directly open to aqueous solution through the movement of a flexible capping loop. The narrow membrane-spanning region of the protease suggests a possible mechanism for accessing scissile bonds that are located near the end of substrate transmembrane helices. Similar principles may apply to the metalloprotease family, where a crystal structure has also become available. Although how the GxGD proteases work it is still less clear, recent results indicate that presenilin also appears to clip substrate from the end of transmembrane helices.
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影响因子：
2.9
作者：
Funamoto, S;Morshima-Kawashima, M;Ihara, Y
通讯作者：
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影响因子：
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作者：
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作者：
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通讯作者：
Ito, K
DOI：
10.1107/s0907444997010457
发表时间：
1998-09-01
影响因子：
2.2
作者：
Cole, LB;Kilpatrick, JM;Babu, YS
通讯作者：
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