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.
- Cyclophilin B (CypB)
- Endoplasmic reticulum
- Lysyl hydroxylase
- Peptidyl prolyl cis-trans-isomerase (PPIase)
- Protein complex
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)