2xgy

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[[Image:2xgy.png|left|200px]]
 
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{{STRUCTURE_2xgy| PDB=2xgy | SCENE= }}
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==Complex of Rabbit Endogenous Lentivirus (RELIK)Capsid with Cyclophilin A==
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<StructureSection load='2xgy' size='340' side='right'caption='[[2xgy]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2xgy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XGY 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]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=2xgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xgy OCA], [https://pdbe.org/2xgy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xgy RCSB], [https://www.ebi.ac.uk/pdbsum/2xgy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xgy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
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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/xg/2xgy_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=2xgy 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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Lentiviruses are widespread in a variety of vertebrates, often associated with chronic disease states. However, until the recent discovery of the prehistoric endogenous lentiviruses in rabbits (RELIK) and lemurs (PSIV), it was thought that lentiviruses had no capacity for germline integration and were only spread horizontally in an exogenous fashion. The existence of RELIK and PSIV refuted these ideas, revealing lentiviruses to be present in a range of mammals, capable of germline integration, and far more ancient than previously thought. Using Gag sequences reconstructed from the remnants of these prehistoric lentiviruses, we have produced chimeric lentiviruses capable of infecting nondividing cells and determined structures of capsid domains from PSIV and RELIK. We show that the structures from these diverse viruses are highly similar, containing features found in modern-day lentiviruses, including a functional cyclophilin-binding loop. Together, these data provide evidence for an ancient capsid-cyclophilin interaction preserved throughout lentiviral evolution.
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===COMPLEX OF RABBIT ENDOGENOUS LENTIVIRUS (RELIK)CAPSID WITH CYCLOPHILIN A===
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Structural and functional analysis of prehistoric lentiviruses uncovers an ancient molecular interface.,Goldstone DC, Yap MW, Robertson LE, Haire LF, Taylor WR, Katzourakis A, Stoye JP, Taylor IA Cell Host Microbe. 2010 Sep 16;8(3):248-59. PMID:20833376<ref>PMID:20833376</ref>
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{{ABSTRACT_PUBMED_20833376}}
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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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==About this Structure==
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<div class="pdbe-citations 2xgy" style="background-color:#fffaf0;"></div>
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[[2xgy]] is a 2 chain structure of [[Cyclophilin]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XGY OCA].
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==See Also==
==See Also==
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*[[Cyclophilin|Cyclophilin]]
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*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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==Reference==
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== References ==
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<ref group="xtra">PMID:020833376</ref><references group="xtra"/>
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Goldstone DC]]
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[[Category: Goldstone, D C.]]
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[[Category: Haire LF]]
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[[Category: Haire, L F.]]
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[[Category: Robertson LE]]
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[[Category: Robertson, L E.]]
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[[Category: Stoye JP]]
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[[Category: Stoye, J P.]]
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[[Category: Taylor IA]]
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[[Category: Taylor, I A.]]
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[[Category: Endogenous]]
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[[Category: Retroviral capsid]]
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[[Category: Viral protein-isomerase complex]]
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Current revision

Complex of Rabbit Endogenous Lentivirus (RELIK)Capsid with Cyclophilin A

PDB ID 2xgy

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