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4WYK

Structure of the LRR and NTF2-like domains of NXF1 complexed with NXT1

Summary for 4WYK
Entry DOI10.2210/pdb4wyk/pdb
DescriptorNuclear RNA export factor 1, NTF2-related export protein 1 (2 entities in total)
Functional Keywordsnuclear export, transport protein
Biological sourceHomo sapiens (Human)
More
Cellular locationNucleus, nucleoplasm : Q9UBU9
Nucleus: Q9UKK6
Total number of polymer chains4
Total formula weight135627.68
Authors
Aibara, S.,Valkov, E.,Stewart, M. (deposition date: 2014-11-17, release date: 2015-02-04, Last modification date: 2024-05-08)
Primary citationAibara, S.,Katahira, J.,Valkov, E.,Stewart, M.
The principal mRNA nuclear export factor NXF1:NXT1 forms a symmetric binding platform that facilitates export of retroviral CTE-RNA.
Nucleic Acids Res., 43:1883-1893, 2015
Cited by
PubMed Abstract: The NXF1:NXT1 complex (also known as TAP:p15) is a general mRNA nuclear export factor that is conserved from yeast to humans. NXF1 is a modular protein constructed from four domains (RRM, LRR, NTF2-like and UBA domains). It is currently unclear how NXF1:NXT1 binds transcripts and whether there is higher organization of the NXF1 domains. We report here the 3.4 Å resolution crystal structure of the first three domains of human NXF1 together with NXT1 that has two copies of the complex in the asymmetric unit arranged to form an intimate domain-swapped dimer. In this dimer, the linkers between the NXF1 LRR and NTF2-like domains interact with NXT1, generating a 2-fold symmetric platform in which the RNA-binding RRM, LRR and NTF2-like domains are arranged on one face. In addition to bulk transcripts, NXF1:NXT1 also facilitates the export of unspliced retroviral genomic RNA from simple type-D retroviruses such as SRV-1 that contain a constitutive transport element (CTE), a cis-acting 2-fold symmetric RNA stem-loop motif. Complementary structural, biochemical and cellular techniques indicated that the formation of a symmetric RNA binding platform generated by dimerization of NXF1:NXT1 facilitates the recognition of CTE-RNA and promotes its nuclear export.
PubMed: 25628361
DOI: 10.1093/nar/gkv032
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.4 Å)
Structure validation

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