A finger-shaped fold in a protein that permits it to interact with DNA and RNA. The fold is created by the binding of specific amino acids in the protein to a zinc atom. Zinc-finger proteins regulate the expression of genes as well as nucleic acid recognition, reverse transcription and virus assembly.

A protein motif consisting of an alpha helix and an anti-parallel beta sheet. Specific amino acids in the helix and sheet interact with a zinc atom, resulting in a finger-like structure.

A DNA binding protein structural motif. Present in many transcription factors (e.g., Sp1, Gal4). The "finger" is formed by 2-4 Cysteine residues and one zinc ion.The protein has repe [..]

A protein structural motif common in DNA binding proteins. Four Cys residues are found for each "finger" and one finger can bind a molecule of zinc. A typical configuration is: CysXxxXxxCys--(intervening 12 or so aa's)--CysXxxXxxCys.

Several types of conserved DNA-binding motifs composed of protein domains folded around a zinc ion; present in several types of eukaryotic transcription factors. (Figure 10-41)

Motifs in DNA- and RNA-Binding Proteins whose Amino Acids are folded into a single structural unit around a Zinc atom. In the classic Zinc finger, one Zinc atom is bound to two cysteines and two histi [..]

A DNA-binding protein motif that contains residues that coordinate a zinc ion which creates a finger-like loop.

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 [..]