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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 PDOC51366
MI domain profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC51366

Description

The MI (after MA-3 and eIF4G) domain is a protein-protein interaction module of ~130 amino acids [1,2,3]. It appears in several translation factors and is found in:

  • One copy in plant and animal eIF4G 1 and 2 (DAP-5/NAT1/p97),
  • Two copies in the animal programmed cell death protein 4 (PDCD4) or MA-3 that is induced during programmed cell death and inhibits neoplastic transformation,
  • Four tandem-repeated copies in a group of uncharacterized plant proteins.

The MI domain consists of seven α-helices, which pack into a globular form (see <PDB:2IOL>). The packing arrangement consists of repeating pairs of antiparallel helices packed one upon the other such that a superhelical axis is generated perpendicular to the α-helical axes [4].

The profile we developed covers the entire MI domain.

Note:

The MI domain has also been named MA3 domain.

Last update:

February 2008 / First entry.

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Technical section

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

MI, PS51366; MI domain profile  (MATRIX)


References

1AuthorsAravind L. Koonin E.V.
TitleEukaryote-specific domains in translation initiation factors: implications for translation regulation and evolution of the translation system.
SourceGenome Res. 10:1172-1184(2000).
PubMed ID10958635

2AuthorsPonting C.P.
TitleNovel eIF4G domain homologues linking mRNA translation with nonsense-mediated mRNA decay.
SourceTrends. Biochem. Sci. 25:423-426(2000).
PubMed ID10973054

3AuthorsYang H.-S. Cho M.-H. Zakowicz H. Hegamyer G. Sonenberg N. Colburn N.H.
TitleA novel function of the MA-3 domains in transformation and translation suppressor Pdcd4 is essential for its binding to eukaryotic translation initiation factor 4A.
SourceMol. Cell. Biol. 24:3894-3906(2004).
PubMed ID15082783

4AuthorsLaRonde-LeBlanc N. Santhanam A.N. Baker A.R. Wlodawer A. Colburn N.H.
TitleStructural basis for inhibition of translation by the tumor suppressor Pdcd4.
SourceMol. Cell. Biol. 27:147-156(2007).
PubMed ID17060447
DOI10.1128/MCB.00867-06



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