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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC51801
Zinc finger CCHC NOA-type profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC51801

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.

Last update:

June 2016 / First entry.

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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



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