HYDROGEN-BOND STEREOCHEMISTRY IN PROTEIN-STRUCTURE AND FUNCTION
HYDROGEN-BOND STEREOCHEMISTRY IN PROTEIN-STRUCTURE AND FUNCTION
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DOI：
10.1016/s0022-2836(05)80364-x
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发表时间：
1990-10-05
影响因子：
5.6
通讯作者：
CHRISTIANSON, DW
中科院分区：
文献类型：
--
作者：
IPPOLITO, JA;ALEXANDER, RS;CHRISTIANSON, DW
从布鲁克海文蛋白质数据库的50个高分辨率蛋白质结构已被分析的氢键立体化学中的反复出现的图案。尽管Baker和Hubbard已经提出了氢键统计的详尽分析，但缺乏对蛋白质内经典供体（N-H、O-H或S-H）和受体（N：、O：或S：）结构的详细立体化学分析。在这里，我们描述了谷氨酸和天冬氨酸（羧酸），谷氨酰胺和天冬酰胺（羧酰胺），精氨酸（胍），组氨酸（咪唑/咪唑），色氨酸（吲哚），酪氨酸（酚羟基），赖氨酸（铵），丝氨酸和苏氨酸（烷基羟基），半胱氨酸（硫醇），蛋氨酸（硫醚）和胱氨酸（二硫化物）的侧链的优先氢键立体化学。优先的氢和立体化学由（1）受体原子的电子构型，（2）供体原子的空间可及性和（3）氨基酸侧链的构象决定。氢键立体化学的应用有助于解释蛋白质的结构、功能和稳定性。此外，这种立体化学是解释蛋白质-其他分子识别和生物催化的先决条件。
Fifty high resolution protein structures from the Brookhaven Protein Data Bank have been analyzed for recurring motifs in hydrogen bond stereochemistry. Although an exhaustive analysis of hydrogen bond statistics has been presented by Baker and Hubbard, a detailed stereochemical analysis of classical donor (N-H, O-H, or S-H) and acceptor (N:, O:, or S:) structure within proteins is lacking. Here, we describe the preferential hydrogen bond stereochemistry for the side-chains of glutamate and aspartate (carboxylate), glutamine and asparagine (carboxamide), arginine (guanidinium), histidine (imidazole/imidazolium), tryptophan (indole), tyrosine (phenolic hydroxyl), lysine (ammonium), serine and threonine (alkyl hydroxyl), cysteine (thiol), methionine (thioether) and cystine (disulfide). Preferential hydrogen ond stereochemistry is governed by (1) the electronic configuration of acceptor atoms, (2) the steric accessibility of donor atoms and (3) the conformation of amino acid side-chains. Applications of hydrogen bond stereochemistry are useful in the interpretation of protein structure, function and stability. Additionally, this stereochemistry is a prerequisite to the interpretation of protein-other molecule recognition and biological catalysis.