4frv | pdb_00004frv

Crystal structure of mutated cyclophilin B that causes hyperelastosis cutis in the American Quarter Horse

spinqualitylabelsall models 4frv, resolution 1.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4frv is a 1 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ME2, PEG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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] 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cyclophilin 3D structures

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