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This method classifies zinc finger proteins into "fold groups" based on the overall shape of the protein backbone in the folded domain. The most common "fold groups" of zinc fingers are the Cys 2 His 2-like (the "classic zinc finger"), treble clef, and zinc ribbon. [19] The following table [19] shows the different structures and their key features:
In molecular biology the B-box-type zinc finger domain is a short protein domain of around 40 amino acid residues in length. B-box zinc fingers can be divided into two groups, where types 1 and 2 B-box domains differ in their consensus sequence and in the spacing of the 7-8 zinc-binding residues.
Zinc finger and BTB domain-containing protein 32 is a protein that in humans is encoded by the 1960 bp ZBTB32 gene.The 52 kDa protein (487 aa) is a transcriptional repressor and the gene is expressed in T and B cells upon activation, but also significantly in testis cells.
The BTB/POZ domain (BTB for BR-C, ttk and bab [2] or POZ for Pox virus and Zinc finger [3]) is a structural domain found in proteins across the domain Eukarya. [4] Given its prevalence in eukaryotes and its absence in Archaea and bacteria, it likely arose after the origin of eukaryotes. [5]
The FYVE domain is composed of two small beta hairpins (or zinc knuckles) followed by an alpha helix. [5] The FYVE finger binds two zinc ions. The FYVE finger has eight potential zinc coordinating cysteine positions and is characterized by having basic amino acids around the cysteines.
Some members of this class of zinc fingers specifically bind the DNA sequence (A/T)GATA(A/G) in the regulatory regions of genes., [1] giving rise to the name of the domain. In these domains, a single zinc ion is coordinated by 4 cysteine residues. [2] [3] NMR studies have shown the core of the Znf to comprise 2 irregular anti-parallel beta ...
LIM domains are protein structural domains, composed of two contiguous zinc fingers, separated by a two-amino acid residue hydrophobic linker. [1] The domain name is an acronym of the three genes in which it was first identified (LIN-11, Isl-1 and MEC-3). [ 2 ]
In molecular biology, a RING (short for Really Interesting New Gene) finger domain is a protein structural domain of zinc finger type which contains a C 3 HC 4 amino acid motif which binds two zinc cations (seven cysteines and one histidine arranged non-consecutively).