1dz5

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[[Image:1dz5.gif|left|200px]]
 
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{{Structure
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==The NMR structure of the 38KDa U1A protein-PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein==
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|PDB= 1dz5 |SIZE=350|CAPTION= <scene name='initialview01'>1dz5</scene>
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<StructureSection load='1dz5' size='340' side='right'caption='[[1dz5]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=A:ADENOSINE-5&#39;-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5&#39;-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5&#39;-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=U:URIDINE-5&#39;-MONOPHOSPHATE'>U</scene>
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<table><tr><td colspan='2'>[[1dz5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DZ5 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE=
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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=1dz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dz5 OCA], [https://pdbe.org/1dz5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dz5 RCSB], [https://www.ebi.ac.uk/pdbsum/1dz5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dz5 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dz5 OCA], [http://www.ebi.ac.uk/pdbsum/1dz5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dz5 RCSB]</span>
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[https://www.uniprot.org/uniprot/SNRPA_HUMAN SNRPA_HUMAN] Binds stem loop II of U1 snRNA. It is the first snRNP to interact with pre-mRNA. This interaction is required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP. In a snRNP-free form (SF-A) may be involved in coupled pre-mRNA splicing and polyadenylation process. Binds preferentially to the 5'-UGCAC-3' motif in vitro.<ref>PMID:9848648</ref>
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dz/1dz5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1dz5 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The status of the poly(A) tail at the 3'-end of mRNAs controls the expression of numerous genes in response to developmental and extracellular signals. Poly(A) tail regulation requires cooperative binding of two human U1A proteins to an RNA regulatory region called the polyadenylation inhibition element (PIE). When bound to PIE RNA, U1A proteins also bind to the enzyme responsible for formation of the mature 3'-end of most eukaryotic mRNAs, poly(A) polymerase (PAP). The NMR structure of the 38 kDa complex formed between two U1A molecules and PIE RNA shows that binding cooperativity depends on helix C located at the end of the RNA-binding domain and just adjacent to the PAP-interacting domain of U1A. Since helix C undergoes a conformational change upon RNA binding, the structure shows that binding cooperativity and interactions with PAP occur only when U1A is bound to its cognate RNA. This mechanism ensures that the activity of PAP enzyme, which is essential to the cell, is only down regulated when U1A is bound to the U1A mRNA.
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'''THE NMR STRUCTURE OF THE 38KDA U1A PROTEIN-PIE RNA COMPLEX REVEALS THE BASIS OF COOPERATIVITY IN REGULATION OF POLYADENYLATION BY HUMAN U1A PROTEIN'''
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The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein.,Varani L, Gunderson SI, Mattaj IW, Kay LE, Neuhaus D, Varani G Nat Struct Biol. 2000 Apr;7(4):329-35. PMID:10742179<ref>PMID:10742179</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1dz5" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The status of the poly(A) tail at the 3'-end of mRNAs controls the expression of numerous genes in response to developmental and extracellular signals. Poly(A) tail regulation requires cooperative binding of two human U1A proteins to an RNA regulatory region called the polyadenylation inhibition element (PIE). When bound to PIE RNA, U1A proteins also bind to the enzyme responsible for formation of the mature 3'-end of most eukaryotic mRNAs, poly(A) polymerase (PAP). The NMR structure of the 38 kDa complex formed between two U1A molecules and PIE RNA shows that binding cooperativity depends on helix C located at the end of the RNA-binding domain and just adjacent to the PAP-interacting domain of U1A. Since helix C undergoes a conformational change upon RNA binding, the structure shows that binding cooperativity and interactions with PAP occur only when U1A is bound to its cognate RNA. This mechanism ensures that the activity of PAP enzyme, which is essential to the cell, is only down regulated when U1A is bound to the U1A mRNA.
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*[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1DZ5 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZ5 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein., Varani L, Gunderson SI, Mattaj IW, Kay LE, Neuhaus D, Varani G, Nat Struct Biol. 2000 Apr;7(4):329-35. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10742179 10742179]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Gunderson, S I.]]
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[[Category: Gunderson SI]]
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[[Category: Kay, L E.]]
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[[Category: Kay LE]]
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[[Category: Mattaj, I W.]]
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[[Category: Mattaj IW]]
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[[Category: Neuhaus, D.]]
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[[Category: Neuhaus D]]
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[[Category: Varani, G.]]
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[[Category: Varani G]]
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[[Category: Varani, L.]]
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[[Category: Varani L]]
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[[Category: polyadenylation]]
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[[Category: protein protein interaction]]
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[[Category: rna protein interaction]]
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[[Category: u1a protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:51:42 2008''
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Current revision

The NMR structure of the 38KDa U1A protein-PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein

PDB ID 1dz5

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