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2xgy

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

Structural highlights

2xgy is a 2 chain structure with sequence from Homo sapiens and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PPIA_HUMAN PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Goldstone DC, Yap MW, Robertson LE, Haire LF, Taylor WR, Katzourakis A, Stoye JP, Taylor IA. Structural and functional analysis of prehistoric lentiviruses uncovers an ancient molecular interface. Cell Host Microbe. 2010 Sep 16;8(3):248-59. PMID:20833376 doi:10.1016/j.chom.2010.08.006

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2xgy"

@@ Line 1: / Line 1: @@
 ==Complex of Rabbit Endogenous Lentivirus (RELIK)Capsid with Cyclophilin A==
-<StructureSection load='2xgy' size='340' side='right' caption='[[2xgy]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='2xgy' size='340' side='right'caption='[[2xgy]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2xgy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit] and [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XGY FirstGlance]. <br>
+<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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
+</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>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vbs|1vbs]], [[1oca|1oca]], [[1mf8|1mf8]], [[2cyh|2cyh]], [[1cwb|1cwb]], [[1vbt|1vbt]], [[1cwl|1cwl]], [[1m9e|1m9e]], [[1cwc|1cwc]], [[1cwo|1cwo]], [[1cwi|1cwi]], [[2x2c|2x2c]], [[1rmh|1rmh]], [[1cwj|1cwj]], [[2rmb|2rmb]], [[1m9c|1m9c]], [[1cwa|1cwa]], [[1cwf|1cwf]], [[3cyh|3cyh]], [[1m9y|1m9y]], [[4cyh|4cyh]], [[1m9f|1m9f]], [[1cwh|1cwh]], [[1bck|1bck]], [[1w8v|1w8v]], [[1awr|1awr]], [[1nmk|1nmk]], [[1mik|1mik]], [[1awv|1awv]], [[1m9d|1m9d]], [[1awt|1awt]], [[2cpl|2cpl]], [[1fgl|1fgl]], [[2x2a|2x2a]], [[1m9x|1m9x]], [[1cwk|1cwk]], [[1m63|1m63]], [[5cyh|5cyh]], [[2x2d|2x2d]], [[1ak4|1ak4]], [[1aws|1aws]], [[2alf|2alf]], [[3cys|3cys]], [[1w8l|1w8l]], [[2x25|2x25]], [[1w8m|1w8m]], [[1awu|1awu]], [[2rma|2rma]], [[1cwm|1cwm]], [[1awq|1awq]], [[2xgu|2xgu]]</td></tr>
+<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>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xgy OCA], [http://pdbe.org/2xgy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xgy RCSB], [http://www.ebi.ac.uk/pdbsum/2xgy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xgy ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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.
+[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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 31: @@
 ==See Also==
-*[[Cyclophilin|Cyclophilin]]
+*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
-*[[Virus coat protein|Virus coat protein]]
+*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: European rabbit]]
+[[Category: Homo sapiens]]
-[[Category: Human]]
+[[Category: Large Structures]]
-[[Category: Peptidylprolyl isomerase]]
+[[Category: Oryctolagus cuniculus]]
-[[Category: Goldstone, D C]]
+[[Category: Goldstone DC]]
-[[Category: Haire, L F]]
+[[Category: Haire LF]]
-[[Category: Robertson, L E]]
+[[Category: Robertson LE]]
-[[Category: Stoye, J P]]
+[[Category: Stoye JP]]
-[[Category: Taylor, I A]]
+[[Category: Taylor IA]]
-[[Category: Endogenous]]
-[[Category: Retroviral capsid]]
-[[Category: Viral protein-isomerase complex]]

2xgy

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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