2jv4: Difference between revisions

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New page: left|200px<br /><applet load="2jv4" size="450" color="white" frame="true" align="right" spinBox="true" caption="2jv4" /> '''Structure Characterisation of PINA WW Domain...
 
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[[Image:2jv4.gif|left|200px]]<br /><applet load="2jv4" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Structure Characterisation of PINA WW Domain and Comparison with other Group IV WW Domains, PIN1 and ESS1'''<br />


==About this Structure==
==Structure Characterisation of PINA WW Domain and Comparison with other Group IV WW Domains, PIN1 and ESS1==
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 superseeds 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2JV4 OCA].  
<StructureSection load='2jv4' size='340' side='right'caption='[[2jv4]]' scene=''>
[[Category: Emericella nidulans]]
== Structural highlights ==
[[Category: Peptidylprolyl isomerase]]
<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>
[[Category: Single protein]]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
[[Category: Brownlee, R.T.C.]]
<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>
[[Category: Kato, Y.]]
</table>
[[Category: Ng, C.A.]]
== Function ==
[[Category: Tanokura, M.]]
[https://www.uniprot.org/uniprot/O42735_EMEND O42735_EMEND]  
[[Category: isomerase]]
== Evolutionary Conservation ==
[[Category: ppiase domain]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: rotamase]]
Check<jmol>
[[Category: ww domain group iv]]
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jv/2jv4_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 08:55:49 2007''
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2jv4" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aspergillus nidulans]]
[[Category: Large Structures]]
[[Category: Brownlee RTC]]
[[Category: Kato Y]]
[[Category: Ng CA]]
[[Category: Tanokura M]]

Latest revision as of 19:06, 29 May 2024

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

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