期刊
MOLECULES
卷 17, 期 6, 页码 7266-7283出版社
MDPI
DOI: 10.3390/molecules17067266
关键词
Protein Data Bank; chalcogen bonds; sigma-hole bonds; molecular assembly; protein engineering; drug design
资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan [15014211, 16014223, 16350092]
- Grants-in-Aid for Scientific Research [16014223, 23550198, 16350092, 15014211] Funding Source: KAKEN
In organic molecules a divalent sulfur atom sometimes adopts weak coordination to a proximate heteroatom (X). Such hypervalent nonbonded S center dot center dot center dot X interactions can control the molecular structure and chemical reactivity of organic molecules, as well as their assembly and packing in the solid state. In the last decade, similar hypervalent interactions have been demonstrated by statistical database analysis to be present in protein structures. In this review, weak interactions between a divalent sulfur atom and an oxygen or nitrogen atom in proteins are highlighted with several examples. S center dot center dot center dot O interactions in proteins showed obviously different structural features from those in organic molecules (i.e., pi(O) -> sigma(S)* versus n(O) -> sigma(S)* directionality). The difference was ascribed to the HOMO of the amide group, which expands in the vertical direction (pO) rather than in the plane (nO). S center dot center dot center dot X interactions in four model proteins, phospholipase A(2) (PLA(2)), ribonuclease A (RNase A), insulin, and lysozyme, have also been analyzed. The results suggested that S center dot center dot center dot X interactions would be important factors that control not only the three-dimensional structure of proteins but also their functions to some extent. Thus, S center dot center dot center dot X interactions will be useful tools for protein engineering and the ligand design.
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