1uw4: Difference between revisions
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[[Image:1uw4. | [[Image:1uw4.jpg|left|200px]]<br /><applet load="1uw4" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1uw4" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1uw4, resolution 1.95Å" /> | caption="1uw4, resolution 1.95Å" /> | ||
'''THE STRUCTURAL BASIS OF THE INTERACTION BETWEEN NONSENSE MEDIATED DECAY FACTORS UPF2 AND UPF3'''<br /> | '''THE STRUCTURAL BASIS OF THE INTERACTION BETWEEN NONSENSE MEDIATED DECAY FACTORS UPF2 AND UPF3'''<br /> | ||
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==Overview== | ==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. | 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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300298 300298]] | |||
==About this Structure== | ==About this Structure== | ||
1UW4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with BME as [http://en.wikipedia.org/wiki/ligand ligand]. | 1UW4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with BME as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Bme Binding Site For Chain D'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UW4 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: rnp domain]] | [[Category: rnp domain]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:14:03 2007'' | ||
Revision as of 19:04, 18 December 2007
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THE STRUCTURAL BASIS OF THE INTERACTION BETWEEN NONSENSE MEDIATED DECAY FACTORS UPF2 AND UPF3
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Mental retardation, X-linked, syndromic 14 OMIM:[300298]
About this StructureAbout this Structure
1UW4 is a Protein complex structure of sequences from Homo sapiens with BME as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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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