AMINO-AROMATIC INTERACTIONS IN PROTEINS
AMINO-AROMATIC INTERACTIONS IN PROTEINS
复制标题
DOI：
10.1016/0014-5793(86)80730-x
复制
发表时间：
1986-07-28
期刊：
影响因子：
3.5
通讯作者：
PETSKO, GA
中科院分区：
文献类型：
--
作者：
BURLEY, SK;PETSKO, GA
对33个精细高分辨率蛋白质晶体结构（2个或更高）的几何分析表明，侧链氨基与芳香侧链相互作用。赖氨酸、精氨酸、天冬酰胺、谷氨酰胺和组氨酸的带正电荷或δ（+）氨基优先位于苯丙氨酸、酪氨酸和色氨酸的环质心的6 π内，在那里它们与δ（-）π电子进行货车范德华接触并避开δ（+）环边缘。这种几何图案不同于预期的分布，这是由于蛋白质中侧链的随机紧密堆积。它与氧-和硫-芳族相互作用相反，类似于芳族-芳族相互作用，并且几乎肯定是静电起源。
Geometric analysis of 33 refined high‐resolution protein crystal structures (2 Å or higher) demonstrates that side‐chain amino groups interact with aromatic side chains. Positively charged or δ(+) amino groups of lysine, arginine, asparagine, glutamine and histidine are preferentially located within 6 Å of the ring centroids of phenylalanine, tyrosine and trytophan, where they make van der Waals' contact with the δ(−) π‐electrons and avoid the δ(+) ring edge. This geometric pattern is different from the distribution expected due to random close packing of side chains in a protein. It is opposite to oxygen‐ and sulfur‐aromatic interactions, similar to aromatic‐aromatic interactions, and almost certainly electrostatic in origin.