Helix packing in membrane proteins
Helix packing in membrane proteins
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DOI：
10.1006/jmbi.1997.1279
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发表时间：
1997-10-10
影响因子：
5.6
通讯作者：
Bowie, JU
中科院分区：
文献类型：
--
作者：
Bowie, JU
对三种独立的跨膜蛋白结构中45个跨膜螺旋和88个跨膜螺旋的相互作用进行了研究，发现了以下特点：（1）受阻的长度范围为14 ~ 36个残基，平均长度为26.4个残基;优选长度大于20个残基。(2)螺旋相对于双层法线平均倾斜21度，但有一个确定的偏好较小的倾斜角。(3)螺旋堆积角的分布与可溶性蛋白质非常不同。TM螺旋最常见的堆积角集中在+20度左右，而可溶性蛋白质的堆积角最普遍为-35度左右。(4)最近距离的平均距离为9.6埃，与可溶性蛋白相同。(5)沿着螺旋长度沿着最接近的点的位置没有偏好（6）TM螺旋在序列中相对于相邻螺旋堆积几乎是一个规则。在37个具有序列邻居的螺旋中，其中36个与邻居显著接触。(7)反平行取向比平行取向更普遍，平均而言，反平行相互作用更密切。螺旋束膜蛋白结构的一般特点，在这次调查中所描述的螺旋束跨膜蛋白的建模应证明是有用的。(C)出版社：Academic Press Limited。
A survey of 45 transmembrane (TM) helices and 88 helix packing interactions In three independent transmembrane protein structures reveals the following features, (1) Helix lengths range from 14 to 36 residues with an average length of 26.4 residues. There is a preference for lengths greater than 20 residues. (2) The helices are tilted with respect to the bilayer normal by an average of 21 degrees, but there is a decided preference for smaller tilt angles. (3) The distribution of helix packing angles is very different than for soluble proteins. The most common packing angles for TM helices are centered around +20 degrees while for soluble proteins packing angles of around -35 degrees are the most prevalent. (4) The average distance of closest approach is 9.6 Angstrom, which is the same as soluble proteins. (5) There is no preference for the positioning of the point of closest approach along the length of the helices (6) It is almost a rule that TM helices pack against: neighbors in the sequence. Of the 37 helices that have a sequence neighbor, 36 of them are in significant contact with a neighbor. (7) An antiparallel orientation is more prevalent than a parallel orientation and antiparallel interactions are more intimate on average. The general features of helix bundle membrane protein architecture described in this survey should prove useful in the modeling of helix bundle transmembrane proteins. (C) 1997 Academic Press Limited.