Structure and Function of CW Domain Containing Proteins

Curr Protein Pept Sci. 2016;17(5):497-506. doi: 10.2174/1389203717666160125115130.

Abstract

The CW domain is a zinc binding domain, composed of approximately 50- 60 amino acid residues with four conserved cysteine (C) and two to four conserved tryptophan (W) residues. The members of the superfamily of CW domain containing proteins, comprised of 12 different eukaryotic nuclear protein families, are extensively expressed in vertebrates, vertebrate-infecting parasites and higher plants, where they are often involved in chromatin remodeling, methylation recognition, epigenetic regulation and early embryonic development. Since the first CW domain structure was determined 5 years ago, structures of five CW domains have been solved so far. In this review, we will discuss these recent advances in understanding the identification, definition, structure, and functions of the CW domain containing proteins.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Arabidopsis Proteins / chemistry
  • Arabidopsis Proteins / metabolism
  • Binding Sites
  • Carrier Proteins / chemistry*
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Conserved Sequence
  • Cysteine* / chemistry
  • Histones / chemistry
  • Histones / metabolism
  • Humans
  • Models, Molecular
  • Multigene Family
  • Protein Binding
  • Protein Conformation
  • Protein Interaction Domains and Motifs*
  • Structure-Activity Relationship
  • Tryptophan* / chemistry
  • Zinc / chemistry*
  • Zinc / metabolism*

Substances

  • Arabidopsis Proteins
  • Carrier Proteins
  • Histones
  • zinc-binding protein
  • Tryptophan
  • Zinc
  • Cysteine