PROSITE documentation PDOC51366MI 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
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References
| 1 | Authors | Aravind L. Koonin E.V. |
| Title | Eukaryote-specific domains in translation initiation factors: implications for translation regulation and evolution of the translation system. | |
| Source | Genome Res. 10:1172-1184(2000). | |
| PubMed ID | 10958635 |
| 2 | Authors | Ponting C.P. |
| Title | Novel eIF4G domain homologues linking mRNA translation with nonsense-mediated mRNA decay. | |
| Source | Trends. Biochem. Sci. 25:423-426(2000). | |
| PubMed ID | 10973054 |
| 3 | Authors | Yang H.-S. Cho M.-H. Zakowicz H. Hegamyer G. Sonenberg N. Colburn N.H. |
| Title | A novel function of the MA-3 domains in transformation and translation suppressor Pdcd4 is essential for its binding to eukaryotic translation initiation factor 4A. | |
| Source | Mol. Cell. Biol. 24:3894-3906(2004). | |
| PubMed ID | 15082783 |
| 4 | Authors | LaRonde-LeBlanc N. Santhanam A.N. Baker A.R. Wlodawer A. Colburn N.H. |
| Title | Structural basis for inhibition of translation by the tumor suppressor Pdcd4. | |
| Source | Mol. Cell. Biol. 27:147-156(2007). | |
| PubMed ID | 17060447 | |
| DOI | 10.1128/MCB.00867-06 |
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