MacKenzie K R, Prestegard J H, Engelman D M
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA.
Science. 1997 Apr 4;276(5309):131-3. doi: 10.1126/science.276.5309.131.
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.
通过对溶解在水性去污剂胶束中的40个残基肽进行溶液核磁共振光谱分析，确定了血型糖蛋白A（GpA）二聚体跨膜结构域的三维结构。GpA跨膜α螺旋以-40度角交叉，形成一个小而紧密堆积的界面，该界面缺乏单体间氢键。该结构为先前表征的GpA二聚化的序列依赖性提供了解释，并证明仅范德华相互作用就可以介导跨膜螺旋之间稳定且特异性的缔合。
