8SRR
Cryo-EM structure of the CBC-ALYREF complex
Summary for 8SRR
Entry DOI | 10.2210/pdb8srr/pdb |
EMDB information | 40739 |
Descriptor | Nuclear cap-binding protein subunit 1, Nuclear cap-binding protein subunit 2, RNA and export factor binding protein 2, ... (4 entities in total) |
Functional Keywords | mrna nuclear export, rna binding protein |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 3 |
Total formula weight | 127989.52 |
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 citation | Clarke, 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: 39282949DOI: 10.7554/eLife.91432 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.22 Å) |
Structure validation
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