InterProInterPro Protein Domain record

Zinc finger, GRF-type
http://metadb.riken.jp/db/SciNetS_rib124i/crib124s1rib124u10666i

Zinc finger, GRF-type

InterPro Protein Domain record

description
  • <p>Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from <taxon tax_id="8355">Xenopus laevis</taxon> (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [<cite idref="PUB00035807"/>, <cite idref="PUB00035805"/>, <cite idref="PUB00035806"/>, <cite idref="PUB00035804"/>, <cite idref="PUB00014077"/>]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few [<cite idref="PUB00035812"/>]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. </p><p>This presumed zinc-binding domain is found in a variety of DNA-binding proteins. It seems likely that this domain is involved in nucleic acid binding. It is named GRF after three conserved residues in the centre of the alignment of the domain. This zinc finger may be related to <db_xref db="INTERPRO" dbkey="IPR000380"/>.</p><p>More information about these proteins can be found at Protein of the Month: Zinc Fingers [<cite idref="PUB00035813"/>].</p>
label
  • Zinc finger, GRF-type
attributionURL
signatures_SMART
type
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contains
PDB_structure
Os_RAPDB_Locus
Pfam-A