1uw4
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Nonsense-mediated mRNA decay (NMD) is a surveillance mechanism by which | + | 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. |
==Disease== | ==Disease== | ||
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[[Category: rnp domain]] | [[Category: rnp domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:59 2008'' |
Revision as of 13:29, 21 February 2008
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THE STRUCTURAL BASIS OF THE INTERACTION BETWEEN NONSENSE MEDIATED DECAY FACTORS UPF2 AND UPF3
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Mental retardation, X-linked, syndromic 14 OMIM:[300298]
About this Structure
1UW4 is a Protein complex structure of sequences from Homo sapiens with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
The structural basis for the interaction between nonsense-mediated mRNA decay factors UPF2 and UPF3., Kadlec J, Izaurralde E, Cusack S, Nat Struct Mol Biol. 2004 Apr;11(4):330-7. Epub 2004 Mar 7. PMID:15004547
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