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2jv4

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[[Image:2jv4.gif|left|200px]]<br /><applet load="2jv4" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2jv4" />
 
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'''Structure Characterisation of PINA WW Domain and Comparison with other Group IV WW Domains, PIN1 and ESS1'''<br />
 
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==About this Structure==
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==Structure Characterisation of PINA WW Domain and Comparison with other Group IV WW Domains, PIN1 and ESS1==
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2JV4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans]. This structure supersedes the now removed PDB entry 2JM7. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JV4 OCA].
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<StructureSection load='2jv4' size='340' side='right'caption='[[2jv4]]' scene=''>
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[[Category: Emericella nidulans]]
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== Structural highlights ==
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[[Category: Peptidylprolyl isomerase]]
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<table><tr><td colspan='2'>[[2jv4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_nidulans Aspergillus nidulans]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2jm7 2jm7]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JV4 FirstGlance]. <br>
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[[Category: Single protein]]
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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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[[Category: Brownlee, R T.C.]]
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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=2jv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jv4 OCA], [https://pdbe.org/2jv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jv4 RCSB], [https://www.ebi.ac.uk/pdbsum/2jv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jv4 ProSAT]</span></td></tr>
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[[Category: Kato, Y.]]
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</table>
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[[Category: Ng, C A.]]
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== Function ==
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[[Category: Tanokura, M.]]
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[https://www.uniprot.org/uniprot/O42735_EMEND O42735_EMEND]
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[[Category: isomerase]]
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== Evolutionary Conservation ==
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[[Category: ppiase domain]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: rotamase]]
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Check<jmol>
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[[Category: ww domain group iv]]
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jv/2jv4_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=2jv4 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 NMR solution structure of the PinA WW domain from Aspergillus nidulans is presented. The backbone of the PinA WW domain is composed of a triple-stranded anti-parallel beta-sheet and an alpha-helix similar to Ess1 and Pin1 without the alpha-helix linker. Large RMS deviations in Loop I were observed both from the NMR structures and molecular dynamics simulation suggest that the Loop I of PinA WW domain is flexible and solvent accessible, thus enabling it to bind the pS/pT-P motif. The WW domain in this structure are stabilised by a hydrophobic core. It is shown that the linker flexibility of PinA is restricted because of an alpha-helical structure in the linker region. The combination of NMR structural data and detailed Molecular Dynamics simulations enables a comprehensive structural and dynamic understanding of this protein.
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:06:05 2008''
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Structural characterisation of PinA WW domain and a comparison with other group IV WW domains, Pin1 and Ess1.,Ng CA, Kato Y, Tanokura M, Brownlee RT Biochim Biophys Acta. 2008 Sep;1784(9):1208-14. Epub 2008 May 8. PMID:18503784<ref>PMID:18503784</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 2jv4" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Aspergillus nidulans]]
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[[Category: Large Structures]]
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[[Category: Brownlee RTC]]
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[[Category: Kato Y]]
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[[Category: Ng CA]]
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[[Category: Tanokura M]]

Current revision

Structure Characterisation of PINA WW Domain and Comparison with other Group IV WW Domains, PIN1 and ESS1

PDB ID 2jv4

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