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Zinc finger (Znf) domains are relatively small protein motifs that bind one or more zinc atoms, and which usually contain multiple finger-like protrusions that make tandem contacts with their target molecule. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis, however they are now recognised to bind DNA, RNA, protein and/or lipid substrates. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superf...
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Authors: Christian B Gocke, Hongtao Yu
PloS one 2008Authors: Christine Brand, Frank Schaeffel, Marita Pauline Feldkaemper
Molecular vision 2007Thought leaders and organizations working on research involving Zinc finger, MYM-type.
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