A transmembrane helix dimer: Structure and implications
A transmembrane helix dimer: Structure and implications
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DOI：
10.1126/science.276.5309.131
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发表时间：
1997-04-04
期刊：
影响因子：
56.9
通讯作者：
Engelman, DM
中科院分区：
文献类型：
--
作者：
MacKenzie, KR;Prestegard, JH;Engelman, DM
通过溶液核磁共振光谱法确定了糖蛋白A（GPA）的二维跨膜结构域的三维结构，该溶液在水溶液胶束中溶解的40个残留肽的核磁共振光谱。 GPA跨膜的α螺旋以-40度的角度交叉，形成一个小但充满包装的界面，缺乏间间氢键。该结构为GPA二聚化的先前表征序列依赖性提供了解释，并证明了单独的范德华相互作用可以介导跨膜螺旋之间的稳定和特定的关联。
The three-dimensional structure of the dimeric transmembrane domain of glycophorin A (GpA) was determined by solution nuclear magnetic resonance spectroscopy of a 40-residue peptide solubilized in aqueous detergent micelles. The GpA membrane-spanning alpha helices cross at an angle of -40 degrees and form a small but well-packed interface that lacks intermonomer hydrogen bonds. The structure provides an explanation for the previously characterized sequence dependence of GpA dimerization and demonstrates that van der Waals interactions alone can mediate stable and specific associations between transmembrane helices.