9UPB
Structure of the human TREX-2 bound to UAP56
Summary for 9UPB
| Entry DOI | 10.2210/pdb9upb/pdb |
| EMDB information | 64390 |
| Descriptor | Germinal-center associated nuclear protein, PCI domain-containing protein 2, 26S proteasome complex subunit SEM1, ... (5 entities in total) |
| Functional Keywords | mrna nuclear export, trex-2, uap56, gene regulation |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 161986.78 |
| Authors | |
| Primary citation | Gong, X.,Tao, R.,Ge, X.,Zhu, H.,Li, M.,Chen, Y.,Gao, Y.,Hang, J.,Zhang, X. Molecular insights into mRNA export regulation by the human TREX-2 complex. Nat Commun, 17:-, 2026 Cited by PubMed Abstract: The nuclear export of mRNA represents a critical regulatory node in eukaryotic gene expression. This process is orchestrated by two conserved multi-subunit assemblies: the transcription-and-export complex (TREX) and TREX-2. While TREX facilitates mRNP packaging through multivalent RNA-protein interactions, the precise mechanism by which TREX-2 contributes to mRNA export has remained elusive. Here, we report a functional interaction between UAP56 and TREX-2 and resolve the structures of TREX-2 in both apo and UAP56-bound states. UAP56 engages TREX-2 via its N-terminal region, positioning its RecA domains on the V-shaped surface of the complex. A conserved loop from TREX-2 inserts between the RecA domains of UAP56, stabilizing an open conformation. Biochemical assays demonstrate that TREX-2 significantly stimulates the ATPase activity of UAP56, thereby promoting RNA release. These findings provide structural and mechanistic insights into TREX-2-mediated regulation of mRNA export through UAP56 remodeling. PubMed: 41748650DOI: 10.1038/s41467-026-70088-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.41 Å) |
Structure validation
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