Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Boudko SP, Ishikawa Y, Lerch TF, Nix J, Chapman MS, Bachinger HP. Crystal structures of wild-type and mutated cyclophilin B that causes hyperelastosis cutis in the American quarter horse. BMC Res Notes. 2012 Nov 8;5:626. doi: 10.1186/1756-0500-5-626. PMID:23137129 doi:http://dx.doi.org/10.1186/1756-0500-5-626
