WHERE METAL-IONS BIND IN PROTEINS

被引:301
作者
YAMASHITA, MM
WESSON, L
EISENMAN, G
EISENBERG, D
机构
[1] UNIV CALIF LOS ANGELES, INST MOLEC BIOL, LOS ANGELES, CA 90024 USA
[2] UNIV CALIF LOS ANGELES, DEPT CHEM & BIOCHEM, LOS ANGELES, CA 90024 USA
[3] UNIV CALIF LOS ANGELES, DEPT PHYSIOL, LOS ANGELES, CA 90024 USA
关键词
Hydrophobicity contrast function; Metalloprotein; Protein structure;
D O I
10.1073/pnas.87.15.5648
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The environments of metal ions (Li+, Na+, K+, Ag+, Cs+, Mg2+, Ca2+, Mn2+, Cu2+, Zn2+) in proteins and other metal-host molecules have been examined. Regardless of the metal and its precise pattern of ligation to the protein, there is a common qualitative feature to the binding site: the metal is ligated by a shell of hydrophilic atomic groups (containing oxygen, nitrogen, or sulfur atoms) and this hydrophilic shell is embedded within a larger shell of Hydrophobic atomic groups (containing carbon atoms). That is, metals bind at centers of high hydrophobicity contrast. This qualitative observation can be described analytically by the hydrophobicity contrast function, C, evaluated from the structure. This function is large and positive for a sphere of hydrophilic atomic groups (characterized by atomic solvation parameters, Δσ, having values < 0) at the center of a larger sphere of hydrophobic atomic groups (characterized by Δσ > 0). In the 23 metal-binding molecules we have examined, the maximum values of the contrast function lie near to observed metal binding sites. This suggests that the hydrophobicity contrast function may be useful for locating, characterizing, and designing metal binding sites in proteins. (.
引用
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页码:5648 / 5652
页数:5
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