4frv
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4frv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FRV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FRV FirstGlance]. <br> | <table><tr><td colspan='2'>[[4frv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FRV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FRV FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ME2:1-ETHOXY-2-(2-METHOXYETHOXY)ETHANE'>ME2</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.1Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ME2:1-ETHOXY-2-(2-METHOXYETHOXY)ETHANE'>ME2</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4frv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4frv OCA], [https://pdbe.org/4frv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4frv RCSB], [https://www.ebi.ac.uk/pdbsum/4frv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4frv ProSAT]</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=4frv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4frv OCA], [https://pdbe.org/4frv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4frv RCSB], [https://www.ebi.ac.uk/pdbsum/4frv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4frv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/A5YBL8_HORSE A5YBL8_HORSE] PPIases accelerate the folding of proteins.[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223] | [https://www.uniprot.org/uniprot/A5YBL8_HORSE A5YBL8_HORSE] PPIases accelerate the folding of proteins.[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | ABSTRACT: BACKGROUND: Hyperelastosis cutis is an inherited autosomal recessive connective tissue disorder. Affected horses are characterized by hyperextensible skin, scarring, and severe lesions along the back. The disorder is caused by a mutation in cyclophilin B. RESULTS: The crystal structures of both wild-type and mutated (Gly6->Arg) horse cyclophilin B are presented. The mutation neither affects the overall fold of the enzyme nor impairs the catalytic site structure. Instead, it locally rearranges the flexible N-terminal end of the polypeptide chain and also makes it more rigid. CONCLUSIONS: Interactions of the mutated cyclophilin B with a set of endoplasmic reticulum-resident proteins must be affected. | ||
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| - | Crystal structures of wild-type and mutated cyclophilin B that causes hyperelastosis cutis in the American quarter horse.,Boudko SP, Ishikawa Y, Lerch TF, Nix J, Chapman MS, Bachinger HP BMC Res Notes. 2012 Nov 8;5:626. doi: 10.1186/1756-0500-5-626. PMID:23137129<ref>PMID:23137129</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4frv" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]] | *[[Cyclophilin 3D structures|Cyclophilin 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of mutated cyclophilin B that causes hyperelastosis cutis in the American Quarter Horse
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