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| {{STRUCTURE_2hwx| PDB=2hwx | SCENE= }} | | {{STRUCTURE_2hwx| PDB=2hwx | SCENE= }} |
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| '''Structure of human SMG6 E1282C PIN domain mutant.'''
| | ===Structure of human SMG6 E1282C PIN domain mutant.=== |
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| ==Overview==
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| SMG6 and SMG5 are essential factors in nonsense-mediated mRNA decay, a conserved pathway that degrades mRNAs with premature translation termination codons. Both SMG5 and SMG6 have been predicted to contain a C-terminal PIN (PilT N-terminus) domain, present in proteins with ribonuclease activity. We have determined the structures of human SMG5 and SMG6 PIN domains. Although they share a similar overall fold related to ribonucleases of the RNase H family, they have local differences at the putative active site. SMG6 has the canonical triad of acidic residues that are crucial in RNase H for nuclease activity, while SMG5 lacks key catalytic residues. The structural differences are reflected at the functional level. Only the PIN domain of SMG6 has degradation activity on single-stranded RNA in vitro. This difference in catalytic activity is conserved in Drosophila, where an SMG6 with an inactive PIN domain inhibits NMD in a dominant-negative manner. Our findings suggest that the NMD machinery has intrinsic nuclease activity that is likely to contribute to the rapid decay of mRNAs that terminate translation prematurely.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17053788}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17053788 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17053788}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: P body]] | | [[Category: P body]] |
| [[Category: Rna degradation]] | | [[Category: Rna degradation]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:48:46 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:51:53 2008'' |
