View source for 4fru


==Crystal structure of horse wild-type cyclophilin B==
<StructureSection load='4fru' size='340' side='right' caption='[[4fru]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4fru]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FRU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FRU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPIB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9796 Equus caballus])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fru OCA], [http://pdbe.org/4fru PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fru RCSB], [http://www.ebi.ac.uk/pdbsum/4fru PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fru ProSAT]</span></td></tr>
</table>
== Function ==
[[http://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-&gt;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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4fru" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Equus caballus]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Bachinger, H P]]
[[Category: Boudko, S P]]
[[Category: Ishikawa, Y]]
[[Category: Chaperone]]
[[Category: Cyclophilin-type ppiase]]
[[Category: Endoplasmic reticulum]]
[[Category: Foldase]]
[[Category: Isomerase]]
[[Category: Lh1 binding]]
[[Category: P3h1-crtap-cypb complex]]
[[Category: Peptidyl-prolyl cis-trans isomerase]]