Determination of helix-helix interactions in membranes by rotational resonance NMR.
Determination of helix-helix interactions in membranes by rotational resonance NMR.
复制标题
通过旋转共振核磁共振测定膜中螺旋-螺旋相互作用。
DOI：
10.1073/pnas.92.2.488
复制
发表时间：
1995
影响因子：
11.1
通讯作者：
Bormann,BJ
中科院分区：
文献类型：
--
作者：
Smith,SO;Bormann,BJ
人血糖蛋白A在红细胞膜上的二聚化是由蛋白质螺旋跨膜区内的特定相互作用所介导的。旋转共振核磁共振为获得膜系统的高分辨率结构数据提供了一种独特的方法，并已被用来通过与跨膜序列相对应的疏水肽来建立血糖素A二聚体中的分子间联系。测量了位于跨膜结构域中间的疏水序列-G79-V80-M81-A82-G83-V84中的[13C]甲基标记与跨二聚体界面沿肽骨架的特定[13C]羰基标记之间的磁化交换率。只有V80(13CH3)与G79(13C=O)和V84(13CH3)与G83(13C=O)之间有显著的磁化交换，表明这些残基以“脊-槽”的方式堆积在二聚体界面上。
Dimerization of human glycophorin A in erythrocyte membranes is mediated by specific interactions within the helical transmembrane domain of the protein. Rotational resonance NMR provides a unique approach for obtaining high-resolution structural data in membrane systems and has been used to establish intermolecular contacts in the glycophorin A dimer by using hydrophobic peptides that correspond to the transmembrane sequence. Magnetization exchange rates were measured between [13C]methyl labels in the hydrophobic sequence -G79-V80-M81-A82-G83-V84- located in the middle of the transmembrane domain and specific [13C]carbonyl labels along the peptide backbone across the dimer interface. Significant magnetization exchange was observed only between V80 (13CH3) and G79 (13C = O) and between V84 (13CH3) and G83 (13C = O), indicating that these residues are packed in the dimer interface in a "ridges-ingrooves" arrangement.