2xgu
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2xgu is ON HOLD until Paper Publication Authors: Goldstone, D.C., Taylor, I.A., Robertson, L.E., Haire, L.F., Stoye, J.P. Description: Structure of...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the N-terminal domain of capsid protein from Rabbit Endogenous Lentivirus (RELIK)== | |
| + | <StructureSection load='2xgu' size='340' side='right'caption='[[2xgu]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2xgu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XGU FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.502Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xgu OCA], [https://pdbe.org/2xgu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xgu RCSB], [https://www.ebi.ac.uk/pdbsum/2xgu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xgu ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xg/2xgu_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=2xgu ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2xgu" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Oryctolagus cuniculus]] | ||
| + | [[Category: Goldstone DC]] | ||
| + | [[Category: Haire LF]] | ||
| + | [[Category: Robertson LE]] | ||
| + | [[Category: Stoye JP]] | ||
| + | [[Category: Taylor IA]] | ||
Current revision
Structure of the N-terminal domain of capsid protein from Rabbit Endogenous Lentivirus (RELIK)
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