1UW4

The structural basis of the interaction between nonsense mediated decay factors UPF2 and UPF3

Summary for 1UW4

• Entry DOI: 10.2210/pdb1uw4/pdb
• Descriptor: UPF3X, REGULATOR OF NONSENSE TRANSCRIPTS 2, BETA-MERCAPTOETHANOL, ... (4 entities in total)
• Functional Keywords: nonsense mediated mrna decay protein, rna-binding protein, nmd, rnp domain, mif4g domain, rna binding protein
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Nucleus: Q9BZI7; Cytoplasm, perinuclear region: Q9HAU5
• Total number of polymer chains: 4
• Total formula weight: 80516.99

Authors

Kadlec, J.,Izaurralde, E.,Cusack, S. (deposition date: 2004-01-29, release date: 2004-03-11, Last modification date: 2024-05-08)

Primary citation

Kadlec, J.,Izaurralde, E.,Cusack, S.
The Structural Basis for the Interaction between Nonsense-Mediated Mrna Decay Factors Upf2 and Upf3
Nat.Struct.Mol.Biol., 11:330-, 2004

PubMed Abstract: Nonsense-mediated mRNA decay (NMD) is a surveillance mechanism by which eukaryotic cells detect and degrade transcripts containing premature termination codons. Three 'up-frameshift' proteins, UPF1, UPF2 and UPF3, are essential for this process in organisms ranging from yeast to human. We present a crystal structure at a resolution of 1.95 A of the complex between the interacting domains of human UPF2 and UPF3b, which are, respectively, a MIF4G (middle portion of eIF4G) domain and an RNP domain (ribonucleoprotein-type RNA-binding domain). The protein-protein interface is mediated by highly conserved charged residues in UPF2 and UPF3b and involves the beta-sheet surface of the UPF3b RNP domain, which is generally used by these domains to bind nucleic acids. We show that the UPF3b RNP does not bind RNA, whereas the UPF2 construct and the complex do. Our results advance understanding of the molecular mechanisms underlying the NMD quality control process.

PubMed: 15004547
DOI: 10.1038/NSMB741

Experimental method

X-RAY DIFFRACTION (1.95 Å)