Home  |  Contact
PROSITE documentation PDOC51801 [for PROSITE entry PS51801]

Zinc finger CCHC NOA-type profile





Description

The regulatory NEMO (NF-kappaB essential modulator) protein has a crucial role in the canonical NF-kappaB signaling pathway notably involved in immune and inflammatory responses, apoptosis and oncogenesis. The regulatory domain is located in the C-terminal half of NEMO and contains a CCHC-type zinc finger (ZF). A similar CCHC-type zinc finger is also found in other regulators of NF-kappaB, such as Optineurin and ABIN2. The CCHC NOA (NEMO Optineurin ABIN2)-type zinc finger has been shown to function as an ubiquitin-binding domain (UBD) [1,2].

The CCHC NOA-type zinc finger consists of a short antiparallel β-sheet, where β1 and β2 strands are connected by a type IV β-turn, and an α-helix (see <PDB:2JVX>). This ββα fold is stabilized by tetrahedral coordination to a zinc ion [1].

The profile we developed covers the entire CCHC NOA-type zinc finger.

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html --------------------------------------------------------------------------------.

Last update:

June 2016 / First entry.

-------------------------------------------------------------------------------

Technical section

PROSITE method (with tools and information) covered by this documentation:

ZF_CCHC_NOA, PS51801; Zinc finger CCHC NOA-type profile  (MATRIX)


References

1AuthorsCordier F. Vinolo E. Veron M. Delepierre M. Agou F.
TitleSolution structure of NEMO zinc finger and impact of an anhidrotic ectodermal dysplasia with immunodeficiency-related point mutation.
SourceJ. Mol. Biol. 377:1419-1432(2008).
PubMed ID18313693
DOI10.1016/j.jmb.2008.01.048

2AuthorsLaplantine E. Fontan E. Chiaravalli J. Lopez T. Lakisic G. Veron M. Agou F. Israel A.
TitleNEMO specifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain.
SourceEMBO J. 28:2885-2895(2009).
PubMed ID19763089
DOI10.1038/emboj.2009.241



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)