Cation-π interactions in protein-protein interfaces
Cation-π interactions in protein-protein interfaces
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DOI：
10.1002/prot.20417
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发表时间：
2005-05-01
影响因子：
2.9
通讯作者：
Golovin, A
中科院分区：
文献类型：
--
作者：
Crowley, PB;Golovin, A
精氨酸是蛋白质-蛋白质界面中丰富的残基。这种残基的重要性与其侧链在分子间相互作用中的多功能性有关。研究了不同种类的蛋白质-蛋白质界面的阳离子- π相互作用。大约一半的蛋白质复合物和三分之一的同型二聚体被发现含有至少一个分子间阳离子- π对。发现精氨酸和酪氨酸之间的相互作用最为丰富。经计算，静电相互作用能平均约为3千卡/摩尔。使用大分子结构数据库（MSD）对胍与芳香族相互作用进行了基于距离的搜索。这项研究揭示了一半的胍：芳香对以共面方式排列。此外，还发现阳离子- π对的阳离子基团经常参与分子间氢键。通过这种方式，精氨酸侧链可以参与多种相互作用，为蛋白间特异性提供了一种机制。因此，阳离子- π相互作用被确定为蛋白质-蛋白质界面的重要贡献者。(c) 2005 Wiley-Liss, Inc。
Arginine is an abundant residue in protein-protein interfaces. The importance of this residue relates to the versatility of its side chain in intermolecular interactions. Different classes of protein-protein interfaces were surveyed for cation-pi interactions. Approximately half of the protein complexes and one-third of the homodimers analyzed were found to contain at least one intermolecular cation-pi pair. Interactions between arginine and tyrosine were found to be the most abundant. The electrostatic interaction energy was calculated to be similar to 3 kcal/mol, on average. A distance-based search of guanidinium:aromatic interactions was also performed using the Macromolecular Structure Database (MSD). This search revealed that half of the guanidinium:aromatic pairs pack in a coplanar manner. Furthermore, it was found that the cationic group of the cation-pi pair is frequently involved in intermolecular hydrogen bonds. In this manner the arginine side chain can participate in multiple interactions, providing a mechanism for inter-protein specificity. Thus, the cation-pi interaction is established as an important contributor to protein-protein interfaces. (c) 2005 Wiley-Liss, Inc.