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  • ligands
  • The only real difference between the classic and variant RING domains, other than the alteration of zinc ligands, is the loss of the small beta-sheet found in RING domains and the replacement of one strand of this sheet with a single turn of helix. (ebi.ac.uk)
  • A particular zinc finger protein's class is determined by this three-dimensional structure, but it can also be recognized based on the primary structure of the protein or the identity of the ligands coordinating the zinc ion. (wikipedia.org)
  • The DNA-binding loop formed by the coordination of these ligands by zinc were thought to resemble fingers, hence the name. (wikipedia.org)
  • motifs
  • Other viruses such as SARS, polio, Ebola, measles, human coxsackie, Dengue, rabies, human hepatitis, human parainfluenza and human respiratory syncytical have similar zinc finger motifs and could potentially benefit from zinc finger inhibitor technology. (wikipedia.org)
  • These motifs contain two peptide units of Cys-X2-Cys-X4-His-X4-Cys (CCHC), where the X represents a substituted amino acid, that make up the zinc (II) ion binding sites. (wikipedia.org)
  • Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. (ebi.ac.uk)
  • Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. (ebi.ac.uk)
  • sequences
  • Without methods to account for this "context dependence", the standard modular assembly procedure often fails unless it is used to recognize sequences of the form (GNN)N. Numerous selection methods have been used to generate zinc-finger arrays capable of targeting desired sequences. (wikipedia.org)
  • histidine
  • The classical RING finger (RING-HC) has a histidine at the fourth coordinating position and a cysteine at the fifth. (ebi.ac.uk)
  • cell
  • In 1994, it was shown that an artificially-constructed three-finger protein can block the expression of an oncogene in a mouse cell line. (wikipedia.org)
  • specific
  • The solution structure of the N-terminal zinc finger of GATA-1 reveals a specific binding face for the transcriptional co-factor FOG. (ebi.ac.uk)
  • arrangement
  • This electrophilic interaction destabilizes the zinc binding site making it easier for the zinc ion to be withdrawn due to the new arrangement of bonds. (wikipedia.org)
  • similar
  • The RING-CH, which is very similar to the classical RING finger, differs from both of these variants in that it has a cys residue in the fourth position and a His in the fifth. (ebi.ac.uk)
  • site
  • Since the CCHC binding site is mutation resistant and involved in the replication of HIV-1, it makes a prime candidate for the prevention of HIV through zinc ejectors. (wikipedia.org)
  • The binding site then performs a disulfide exchange, forming new intermolecular disulfide bonds, and rearrangement occurs placing the zinc finger in a conformation that inhibits its function. (wikipedia.org)