Senes A, Ubarretxena-Belandia I, Engelman D M
Department of Molecular Biophysics and Biochemistry, Yale University, P.O. Box 208114, New Haven, CT 06520, USA.
Proc Natl Acad Sci U S A. 2001 Jul 31;98(16):9056-61. doi: 10.1073/pnas.161280798.
The Calpha---H...O hydrogen bond has been given little attention as a determinant of transmembrane helix association. Stimulated by recent calculations suggesting that such bonds can be much stronger than has been supposed, we have analyzed 11 known membrane protein structures and found that apparent carbon alpha hydrogen bonds cluster frequently at glycine-, serine-, and threonine-rich packing interfaces between transmembrane helices. Parallel right-handed helix-helix interactions appear to favor Calpha---H...O bond formation. In particular, Calpha---H...O interactions are frequent between helices having the structural motif of the glycophorin A dimer and the GxxxG pair. We suggest that Calpha---H...O hydrogen bonds are important determinants of stability and, depending on packing, specificity in membrane protein folding.
作为跨膜螺旋缔合的一个决定因素,Cα---H...O氢键一直未受到太多关注。受近期计算结果的启发,这些计算表明此类氢键可能比人们认为的要强得多,我们分析了11种已知的膜蛋白结构,发现明显的碳α氢键经常聚集在跨膜螺旋之间富含甘氨酸、丝氨酸和苏氨酸的堆积界面处。平行的右手螺旋-螺旋相互作用似乎有利于Cα---H...O键的形成。特别是,在具有血型糖蛋白A二聚体和GxxxG基序结构基序的螺旋之间,Cα---H...O相互作用很常见。我们认为Cα---H...O氢键是稳定性的重要决定因素,并且根据堆积情况,也是膜蛋白折叠中特异性的重要决定因素。