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8SRR

Cryo-EM structure of the CBC-ALYREF complex

Summary for 8SRR
Entry DOI10.2210/pdb8srr/pdb
EMDB information40739
DescriptorNuclear cap-binding protein subunit 1, Nuclear cap-binding protein subunit 2, RNA and export factor binding protein 2, ... (4 entities in total)
Functional Keywordsmrna nuclear export, rna binding protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains3
Total formula weight127989.52
Authors
Xie, Y.,Clarke, B.P.,Ren, Y. (deposition date: 2023-05-06, release date: 2024-09-25, Last modification date: 2024-10-02)
Primary citationClarke, B.P.,Angelos, A.E.,Mei, M.,Hill, P.S.,Xie, Y.,Ren, Y.
Cryo-EM structure of the CBC-ALYREF complex.
Elife, 12:-, 2024
Cited by
PubMed Abstract: In eukaryotes, RNAs transcribed by RNA Pol II are modified at the 5' end with a 7-methylguanosine (mG) cap, which is recognized by the nuclear cap binding complex (CBC). The CBC plays multiple important roles in mRNA metabolism, including transcription, splicing, polyadenylation, and export. It promotes mRNA export through direct interaction with a key mRNA export factor, ALYREF, which in turn links the TRanscription and EXport (TREX) complex to the 5' end of mRNA. However, the molecular mechanism for CBC-mediated recruitment of the mRNA export machinery is not well understood. Here, we present the first structure of the CBC in complex with an mRNA export factor, ALYREF. The cryo-EM structure of CBC-ALYREF reveals that the RRM domain of ALYREF makes direct contact with both the NCBP1 and NCBP2 subunits of the CBC. Comparing CBC-ALYREF with other cellular complexes containing CBC and/or ALYREF components provides insights into the coordinated events during mRNA transcription, splicing, and export.
PubMed: 39282949
DOI: 10.7554/eLife.91432
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.22 Å)
Structure validation

237735

数据于2025-06-18公开中

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