Structural highlights
Function
[MEX67_YEAST] Involved in the export of mRNA from the nucleus to the cytoplasm.[1] [MTR2_YEAST] Affects mRNA transport from the nucleus to the cytoplasm.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The association between Mtr2 and Mex67 is essential for the nuclear export of bulk messenger RNA in yeast. In metazoans, the analogous function is carried out by the TAP-p15 heterodimer. Whereas Mex67 and TAP are highly conserved proteins, their binding partners, Mtr2 and p15, share no sequence similarity, but are nevertheless functionally homologous. Here, we report the 2.8-A resolution crystal structure of Mtr2 in complex with the NTF2-like domain of Mex67. Mtr2 is a novel member of the NTF2-like family and interacts with Mex67, forming a complex with a similar structural architecture to that of TAP-p15. Mtr2 fulfils an analogous function to that of human p15 in maintaining the structural integrity of the heterodimer. In addition, Mtr2 presents a long internal loop, which contains residues that affect the export of the large ribosomal subunit.
Structural similarity in the absence of sequence homology of the messenger RNA export factors Mtr2 and p15.,Fribourg S, Conti E EMBO Rep. 2003 Jul;4(7):699-703. PMID:12835756[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Segref A, Sharma K, Doye V, Hellwig A, Huber J, Luhrmann R, Hurt E. Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+ RNA and nuclear pores. EMBO J. 1997 Jun 2;16(11):3256-71. PMID:9214641 doi:http://dx.doi.org/10.1093/emboj/16.11.3256
- ↑ Fribourg S, Conti E. Structural similarity in the absence of sequence homology of the messenger RNA export factors Mtr2 and p15. EMBO Rep. 2003 Jul;4(7):699-703. PMID:12835756 doi:10.1038/sj.embor.embor883
