Packing of aromatic rings against tryptophan residues in proteins
Packing of aromatic rings against tryptophan residues in proteins
复制标题
DOI：
10.1107/s090744499900726x
复制
发表时间：
1999-08-01
期刊：
影响因子：
--
通讯作者：
Chakrabarti, P
中科院分区：
文献类型：
--
作者：
Samanta, U;Pal, D;Chakrabarti, P
苯丙氨酸（Phe），酪氨酸（Tyr），色氨酸（Trp）和组氨酸（His）的芳香族侧链与吲哚环的色氨酸的相互作用的几何形状已被分析使用的结构在蛋白质数据库中，以了解依赖的包装行为的大小和化学性质的芳香环。Phe环倾向于垂直地相互作用，其边缘指向Trp面，或以偏移堆叠的方式相互作用。边对面基序是典型的Trp-Trp对。虽然平行堆积是Trp-His相互作用的主要特征，但Tyr以更均匀的方式围绕Trp堆积，在边缘处的发生率高于预期，并且可能存在OH-pi相互作用的少数情况。
The geometry of the interaction of the aromatic side chains of phenylalanine (Phe), tyrosine (Tyr), tryptophan (Trp) and histidine (His) with the indole ring of Trp has been analyzed using the structures in the Protein Data Bank in order to understand the dependence of the packing behaviour on the size and chemical nature of the aromatic rings. The Phe ring prefers to interact either perpendicularly, with its edge pointing towards the Trp face, or in an offset-stacked arrangement. The edge-to-face motif is typical of a Trp-Trp pair. While parallel stacking is the dominant feature of Trp-His interaction, Tyr packs in a more uniform manner around Trp with a higher than expected occurrence at the edge and a few cases of possible OH-pi interaction.