作者: Aaron Klug , John W. R. Schwabe
DOI: 10.1096/FASEBJ.9.8.7768350
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摘要: The term zinc finger was first used to describe a 30-residue, repeated sequence motif found in an unusually abundant Xenopus transcription factor. It proposed that each is folded around central ion form independent minidomain and adjacent fingers are combined as modules make up DNA-binding domain with the "gripping" DNA (hence finger). We now know these proposals were correct motifs many eukaryotic proteins. More recently, crystal structures of three different complexes between domains their target binding sites have revealed remarkably simple mode interaction DNA. simplicity structure, its DNA, very striking feature this protein domain. After discovery motif, patterns potential ligands been several other proteins, some which also bind Structural studies how can stabilize quite diverse architectures. In total, 10 such small zinc-binding studied structurally. These collection, but turn has termed motif-although clearly what they common only property, stabilizes apparently autonomously unit.