2a1s: Difference between revisions

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==Crystal structure of native PARN nuclease domain==
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<StructureSection load='2a1s' size='340' side='right'caption='[[2a1s]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2a1s]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The February 2007 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Exosomes''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2007_2 10.2210/rcsb_pdb/mom_2007_2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A1S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A1S FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a1s OCA], [https://pdbe.org/2a1s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a1s RCSB], [https://www.ebi.ac.uk/pdbsum/2a1s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a1s ProSAT]</span></td></tr>
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== Function ==
[https://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>
== Evolutionary Conservation ==
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    <text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2a1s ConSurf].
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== Publication Abstract from PubMed ==
Poly(A)-specific ribonuclease (PARN) is a processive, poly(A)-specific 3' exoribonuclease. The crystal structure of C-terminal truncated human PARN determined in two states (free and RNA-bound forms) reveals that PARNn is folded into two domains, an R3H domain and a nuclease domain similar to those of Pop2p and epsilon186. The high similarity of the active site structures of PARNn and epsilon186 suggests that they may have a similar catalytic mechanism. PARNn forms a tight homodimer, with the R3H domain of one subunit partially enclosing the active site of the other subunit and poly(A) bound in a deep cavity of its nuclease domain in a sequence-nonspecific manner. The R3H domain and, possibly, the cap-binding domain are involved in poly(A) binding but these domains alone do not appear to contribute to poly(A) specificity. Mutations disrupting dimerization abolish both the enzymatic and RNA-binding activities, suggesting that the PARN dimer is a structural and functional unit. The cap-binding domain may act in concert with the R3H domain to amplify the processivity of PARN.


===Crystal structure of native PARN nuclease domain===
Structural insight into poly(A) binding and catalytic mechanism of human PARN.,Wu M, Reuter M, Lilie H, Liu Y, Wahle E, Song H EMBO J. 2005 Dec 7;24(23):4082-93. Epub 2005 Nov 10. PMID:16281054<ref>PMID:16281054</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 16281054 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_16281054}}
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</StructureSection>
==About this Structure==
2A1S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Additional information on 2A1S is available in a page on [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb86_1.html Exosomes] at the RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A1S OCA].
 
==Reference==
Structural insight into poly(A) binding and catalytic mechanism of human PARN., Wu M, Reuter M, Lilie H, Liu Y, Wahle E, Song H, EMBO J. 2005 Dec 7;24(23):4082-93. Epub 2005 Nov 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16281054 16281054]
[[Category: Exosomes]]
[[Category: Exosomes]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Song, H.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Wu, M.]]
[[Category: Song H]]
[[Category: Dedd]]
[[Category: Wu M]]
[[Category: Nuclease domain]]
[[Category: Parn]]
[[Category: R3h]]
 
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