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PROSITE documentation PDOC51366 |
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:
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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PROSITE method (with tools and information) covered by this documentation:
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 |