SULFUR-AROMATIC INTERACTIONS IN PROTEINS
SULFUR-AROMATIC INTERACTIONS IN PROTEINS
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DOI：
10.1016/0014-5793(85)81285-0
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发表时间：
1985-01-01
期刊：
影响因子：
3.5
通讯作者：
THORNTON, JM
中科院分区：
文献类型：
--
作者：
REID, KSC;LINDLEY, PF;THORNTON, JM
使用来自 36 种蛋白质的晶体学数据分析了球状蛋白质中硫-芳香族相互作用的几何形状，分辨率达到 2 Å 或更高。半胱氨酸和甲硫氨酸残基中约一半的硫原子与芳香环（苯丙氨酸、酪氨酸或色氨酸）接触（距离环质心≤ 6 Å）。与碳和氮原子相比，相互作用的硫原子表现出对芳香环边缘的亲和力，并避开环上方π电子附近的区域。这种偏好类似于之前发现的苯丙氨酸环周围氧原子的偏好，并且可能是静电起源的。硫-芳族相互作用蛋白质侧链接触半胱氨酸蛋氨酸包装
The geometry of sulphur-aromatic interactions in globular proteins has been analysed using crystallographic data derived from 36 proteins, solved to resolutions of 2 Å or better. About half of all sulphur atoms from cyst(e)ine and methionine residues are in contact ( ≦ 6 Å from ring centroid) with an aromatic ring (phenylalanine, tyrosine or tryptophan). Compared to carbon and nitrogen atoms the interacting sulphur atoms express an affinity towards the edge of the aromatic rings, and avoid the region above the ring in the vicinity of the π-electrons. This preference is similar to that previously found for oxygen atoms around phenylalanine rings, and may be electrostatic in origin.Sulfw-aromatic interactionProteinSide-chain contactCyst(e)ineMethioninePacking