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... > Chemical Phenomena > Biochemical Phenomena > Molecular Structure > Molecular Conformation > Protein Conformation > Protein Structural Elements > Amino Acid Motifs > Zinc Fingers > PHD Zinc Fingers
... > Chemical Phenomena > Biochemical Phenomena > Molecular Structure > Molecular Conformation > Protein Conformation > Protein Structure, Secondary > Amino Acid Motifs > Zinc Fingers > PHD Zinc Fingers

Preferred term

PHD Zinc Fingers  

Type

  • Topical Descriptor

Broader concept

Related concepts

Entry terms

  • Domain, PHD
  • Domain, PHD Finger
  • Domains, PHD
  • Domains, PHD Finger
  • Finger Domain, PHD
  • Finger Domains, PHD
  • Finger, PHD
  • Fingers, PHD
  • Motif, PHD
  • Motifs, PHD
  • PHD Domain
  • PHD Domains
  • PHD Finger
  • PHD Finger Domain
  • PHD Finger Domains
  • PHD Fingers
  • PHD Motif
  • PHD Motifs
  • PHD Zinc Finger

Scope note

  • Zinc finger domains of approximately 50 to 80 amino acids in length that are characterized by a conserved Cysteine(3)-Histidine-Cysteine(4) amino acid motif which coordinates binding of two zinc ions. They are similar structurally to RING FINGER DOMAINS, with a globular fold topology of two BETA-SHEETS and an ALPHA-HELIX. PHD fingers occur in many proteins that function in chromatin-mediated gene expression and EPIGENETICS such as POLYCOMB-GROUP PROTEINS.

History note

  • 2018

In other languages

URI

http://www.yso.fi/onto/mesh/D000075925

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