3ctr

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[[Image:3ctr.png|left|200px]]
 
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{{STRUCTURE_3ctr| PDB=3ctr | SCENE= }}
{{STRUCTURE_3ctr| PDB=3ctr | SCENE= }}
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===Crystal structure of the RRM-domain of the poly(A)-specific ribonuclease PARN bound to m7GTP===
===Crystal structure of the RRM-domain of the poly(A)-specific ribonuclease PARN bound to m7GTP===
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{{ABSTRACT_PUBMED_18694759}}
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{{ABSTRACT_PUBMED_18694759}}
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==Function==
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[[http://www.uniprot.org/uniprot/PARN_HUMAN PARN_HUMAN]] 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization.<ref>PMID:9736620</ref> <ref>PMID:10882133</ref> <ref>PMID:11359775</ref> <ref>PMID:12748283</ref> <ref>PMID:15175153</ref>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:018694759</ref><references group="xtra"/>
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<ref group="xtra">PMID:018694759</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Dickmanns, A.]]
[[Category: Dickmanns, A.]]

Revision as of 06:27, 6 November 2013

Template:STRUCTURE 3ctr

Contents

Crystal structure of the RRM-domain of the poly(A)-specific ribonuclease PARN bound to m7GTP

Template:ABSTRACT PUBMED 18694759

Function

[PARN_HUMAN] 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization.[1] [2] [3] [4] [5]

About this Structure

3ctr is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Monecke T, Schell S, Dickmanns A, Ficner R. Crystal structure of the RRM domain of poly(A)-specific ribonuclease reveals a novel m(7)G-cap-binding mode. J Mol Biol. 2008 Oct 17;382(4):827-34. Epub 2008 Jul 31. PMID:18694759 doi:10.1016/j.jmb.2008.07.073
  1. ↑ Korner CG, Wormington M, Muckenthaler M, Schneider S, Dehlin E, Wahle E. The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes. EMBO J. 1998 Sep 15;17(18):5427-37. PMID:9736620 doi:http://dx.doi.org/10.1093/emboj/17.18.5427
  2. ↑ Gao M, Fritz DT, Ford LP, Wilusz J. Interaction between a poly(A)-specific ribonuclease and the 5' cap influences mRNA deadenylation rates in vitro. Mol Cell. 2000 Mar;5(3):479-88. PMID:10882133
  3. ↑ Martinez J, Ren YG, Nilsson P, Ehrenberg M, Virtanen A. The mRNA cap structure stimulates rate of poly(A) removal and amplifies processivity of degradation. J Biol Chem. 2001 Jul 27;276(30):27923-9. Epub 2001 May 18. PMID:11359775 doi:http://dx.doi.org/10.1074/jbc.M102270200
  4. ↑ Lai WS, Kennington EA, Blackshear PJ. Tristetraprolin and its family members can promote the cell-free deadenylation of AU-rich element-containing mRNAs by poly(A) ribonuclease. Mol Cell Biol. 2003 Jun;23(11):3798-812. PMID:12748283
  5. ↑ Gherzi R, Lee KY, Briata P, Wegmuller D, Moroni C, Karin M, Chen CY. A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery. Mol Cell. 2004 Jun 4;14(5):571-83. PMID:15175153 doi:http://dx.doi.org/10.1016/j.molcel.2004.05.002

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