• 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)
  • 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)
  • terminus
  • For example, the human protein Znf216 has an A20 zinc-finger at the N terminus and an AN1 zinc-finger at the C terminus, acting to negatively regulate the NFkappaB activation pathway and to interact with components of the immune response like RIP, IKKgamma and TRAF6. (wikipedia.org)
  • transcription
  • As zinc fingers are known to be involved in m-RNA regulation, reverse transcription, protection of synthesized viral DNA, transcription inhibition, and initial integration processes, prevention of zinc finger function can have drastic effects on the function of the cell or virus. (wikipedia.org)
  • Structural analysis of the recognition of the negative regulator NmrA and DNA by the zinc finger from the GATA-type transcription factor AreA. (ebi.ac.uk)
  • terminal
  • 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)
  • domains
  • This entry represents C-x8-C-x5-C-x3-H (CCCH) type Zinc finger (Znf) domains. (ebi.ac.uk)
  • therefore, both zinc-finger domains are involved in regulating the immune response. (wikipedia.org)
  • AN1-type zinc finger domains are widely present across diverse euryarchaeota and thaumarchaeota, where they are often fused to membrane-associated peptidase domains such as the rhomboid family serine peptidase, transglutaminase-like thiol peptidases of the papain fold, and Zn-dependent metallopeptidases. (wikipedia.org)
  • The architectural syntax is remarkably similar to that of the prokaryotic B-box zinc finger and LIM domains. (wikipedia.org)
  • Zinc fingers fused to various other effector domains, some with therapeutic significance, have since been constructed. (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)
  • 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)