zinc finger
configuratIon of a DNA-binding protein that resembles a finger with a base, usually Cysteines and Histidines, binding a zinc Ion. Discovered in a transcriptIon factor in Xenopus but present in a large number of different proteins. Below is from http://www.biochem.ucl.ac.uk/bsm/prot_DNA/family_descriptIons/zincfinger_family/zincfinger_family.htmlCharacteristics of the family:FunctIon: The DNA-binding motif is found as part of transcriptIon regulatory proteins. Structure: One of the most abundant DNA-binding motifs. proteins may contain more than one finger in a single chain; each motif consists of 2 antiparallel beta-strands followed by by an alpha-helix. A single zinc Ion is tetrahedrally coordinated by conserved Histidine and Cysteine residues, stabilising the motif.Binding: Fingers bind to 3 base-pair subsites and specific contacts are mediated by Amino acids in positIons -1, 2, 3 and 6 relative to the start of the alpha-helix. Contacts mainly involve one strand of the DNA. Where proteins contain multiple fingers, each finger binds to adjacent subsites within a larger DNA recognitIon site thus allowing a relatively simple motif to specifically bind to a wide range of DNA sequences.
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