Cys2his2 zinc finger
WebMay 5, 2004 · This protein consists of three Cys 2 His 2 zinc fingers joined by a pair of Thr- Gly-Glu-Lys-Pro linkers. The individual zinc finger domains are based on the consensus zinc finger peptide CP-1, representing an average zinc finger sequence ( 17 ). Web2.3 Class: Cys2His2 zinc finger domain 2.3.1 Family: Ubiquitous factors, includes TFIIIA, Sp1; 2.3.2 Family: Developmental / cell cycle regulators; includes Krüppel; 2.3.4 Family: Large factors with NF-6B-like binding properties; 2.4 Class: Cys6 cysteine-zinc cluster; 2.5 Class: Zinc fingers of alternating composition; 3 Superclass: Helix-turn ...
Cys2his2 zinc finger
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WebZinc finger nuclease (ZFN) technology utilizes a FokI nuclease as the DNA-cleavage domain and binds DNA by engineered Cys2His2 zinc fingers. Specific zinc fingers recognize different nucleotide triplets and dimerize the FokI nuclease. The activated nuclease introduces a double stranded break between the two distinct zinc finger … WebFeb 1, 2001 · The Cys2His2 zinc finger motif and the Zif268 finger sequences. (Top) A ribbon diagram of finger 2 from Zif268 (8), including the two cysteine side chains (yellow) and two histidine side chains ...
WebJan 9, 2024 · So far, zinc finger motifs have been classified into eight different categories according to their main-chain conformation and secondary structure around their zinc-binding sites, including Cys2His2 (C2H2) like, Zn2/Cys6, Treble clef, Zinc ribbon, Gag knuckle, TAZ2 domain like, Zinc binding loops and Metallothionein [3, 4]. In addition to … WebSep 16, 2011 · The crystal structure of the C2H2 zinc finger of DPF2 (residues D206-H232) is well defined. The overall structure exhibits a canonical C2H2 fold, which contains a short antiparallel β-sheet, where β1 (209–211) and β2 (215–218) strands are connected by β-turn (C 211 DIC 214) and a α helix (221–230).
WebApr 8, 2024 · Since zinc finger proteins are highly homologous to KLF in the DNA-binding region, ... Pabo CO. DNA recognition by Cys2His2 zinc finger proteins. Annu Rev Biophys Biomol Struct. 2000;29:183–212. WebThe Cys2His2 zinc finger motif is a versatile scaffold for the recognition of a variety of different DNA sequences. Using the sequence of Zif268 as a framework zinc fingers with novel specificities have been created by …
WebJan 15, 2015 · Cys 2 His 2 zinc fingers (C2H2-ZFs) comprise the largest class of metazoan DNA-binding domains. Despite this domain's well-defined DNA-recognition interface, and its successful use in the design of chimeric proteins capable of targeting genomic regions of interest, much remains unknown about its DNA-binding landscape.
WebNov 21, 2012 · Cys2His2 zinc-fingers are DNA-binding domains that recognize approximately three base pairs of DNA. Alteration of a small number of residues in or near an α-helix within this domain can lead... shareme uptodownWebJun 28, 2024 · In particular, we analyzed Cys2His2 zinc finger genes, as they comprise the largest family of transcription factors in human. We aggregated somatic mutations within these genes by their positions within zinc finger domains, and found that two specific positions within zinc finger domains are recurrently mutated in three cancer … shareme to pcWebNov 10, 2005 · In these studies, the Cys2His2 zinc finger was chosen as a model for understanding how the gold (I) (Au1+) drug, aurothiomalate (AuTM), interacts … shareme webshareWebZIF268, a member of the classical zinc finger protein family, contains three Cys2His2 zinc binding domains that together recognize the DNA sequence 5′-AGCGTGGGCGT-3′. … share me websiteWebFeb 1, 2000 · Cys2His2 zinc fingers are one of the most common DNA-binding motifs found in eukaryotic transcription factors. These proteins typically contain several fingers that make tandem contacts... shareme wienWebThe zinc finger domain is generally between 23 and 28 amino acids long and is stabilized by coordinating zinc ions with regularly spaced zinc-coordinating residues (either histidines or cysteines). The most common class of zinc finger (Cys2His2) coordinates a single zinc ion and consists of a recognition helix and a 2-strand beta-sheet. [6] share messagesWebThe Cys 2 His 2 (C2H2) zinc finger is one of the simplest independently folded structural domains known, yet the number of proteins with distinct and complex functions that contain the motif is too large to count. The domain consists of a small antiparallel β-sheet and a single helix that contribute two cysteine and two histidine ligands respectively to … shareme win10