RING finger domain

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"RING" redirects here. For other uses, see Ring.
Zinc finger, C3HC4 type (RING finger)
SCOP2
1chc / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In

ubiquitination
pathway.

Zinc fingers

Main article: Zinc finger

Zinc finger (Znf)

protein motifs that bind one or more zinc atoms, and which usually contain multiple finger-like protrusions that make tandem contacts with their target molecule. They bind DNA, RNA, protein and/or lipid substrates.[6][7][8][9][10]
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.[11]
Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.

Some Zn finger domains have diverged such that they still maintain their core structure, but have lost their ability to bind zinc, using other means such as salt bridges or binding to other metals to stabilise the finger-like folds.

Function

Many RING finger domains simultaneously bind ubiquitination enzymes and their substrates and hence function as ligases. Ubiquitination in turn targets the substrate protein for degradation.[12][13][14]

Structure

The RING finger domain has the consensus sequence C-X2-C-X[9-39]-C-X[1-3]-H-X[2-3]-C-X2-C-X[4-48]-C-X2-C.[2] where:

  • C is a conserved cysteine residue involved zinc coordination,
  • H is a conserved histidine involved in zinc coordination,
  • Zn is zinc atom, and
  • X is any amino acid residue.

The following is a schematic representation of the structure of the RING finger domain:[2] 

                              x x x     x x x
                             x      x x      x
                            x       x x       x
                           x        x x        x
                          C        C   C        C
                         x  \    / x   x \    /  x
                         x    Zn   x   x   Zn    x
                          C /    \ H   C /    \ C
                          x         x x         x
                 x x x x x x         x         x x x x x x

Examples

Examples of human genes which encode proteins containing a RING finger domain include:

TRIM5, TRIM6, TRIM7, TRIM8, TRIM9, TRIM10, TRIM11, TRIM13, TRIM15, TRIM17, TRIM21, TRIM22, TRIM23, TRIM24, TRIM25, TRIM26, TRIM27, TRIM28, TRIM31, TRIM32, TRIM33, TRIM34, TRIM35, TRIM36, TRIM38, TRIM39, TRIM40, TRIM41, TRIM42, TRIM43, TRIM45, TRIM46, TRIM47, TRIM48, TRIM49, TRIM50, TRIM52, TRIM54, TRIM55, TRIM56, TRIM58, TRIM59, TRIM60, TRIM61, TRIM62, TRIM63, TRIM65, TRIM67, TRIM68, TRIM69, TRIM71, TRIM72, TRIM73, TRIM74, TRIML1, TTC3, UHRF1, UHRF2, VPS11, VPS8, ZNF179, ZNF294, ZNF313, ZNF364, ZNF451, ZNF650, ZNFB7, ZNRF1, ZNRF2, ZNRF3, ZNRF4, and ZSWIM2
.

References

  1. PMID 8126734
    .
  2. ^
    PMID 8804826
    .
  3. PMID 1906426
    .
  4. PMID 1991318
    .
  5. PMID 7681583
    .
  6. PMID 10529348
    .
  7. PMID 15963892
    .
  8. PMID 15718139
    .
  9. PMID 17210253
    .
  10. S2CID 22109146
    .
  11. PMID 11179890
    .
  12. PMID 10500182
    .
  13. PMID 11007473
    .
  14. PMID 10662664
    .

External links
This article incorporates text from the public domain Pfam and InterPro: IPR001841
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