Zinc finger, FCS-type (IPR012313)
Short name: Znf_FCS
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 Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [PMID: 10529348, PMID: 15963892, PMID: 15718139, PMID: 17210253, PMID: 12665246]. 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 [PMID: 11179890]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.
The FCS-type zinc finger, named after the signature FCS residues associated with the third cysteine, is present in several polycomb group proteins. The FCS zinc finger is expected to adopt a Zn-ribbon like fold. Molecular data suggest that this domain can bind RNA in a non-sequence-specific manner [PMID: 15200961].
Proteins known to contain an FCS-type zinc finger include:
- Drosphila polyhomeotic (ph) protein and vertebrate homologues. They are members of the Polycomb repressive complex 1 (PRC1), an inhibitory complex that acts by preventing chromatin remodeling and transcription.
- Drosophila Sex comb on midleg (Scm) and vertebrate homologues. They are also members of the PRC1.
- Drosphila Lethal(3) malignant brain tumor (l(3)mbt) protein and vertebrate homologues.
- PS51024 (ZF_FCS)