Crystal structures of wild-type and mutated cyclophilin B that causes hyperelastosis cutis in the American quarter horse

Sergei P. Boudko, Yoshihiro Ishikawa, Thomas F. Lerch, Jay Nix, Michael S. Chapman, Hans Peter Bächinger

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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.

Original languageEnglish (US)
Article number626
JournalBMC Research Notes
StatePublished - Nov 12 2012



  • Calreticulin
  • Chaperone
  • Collagen
  • Cyclophilin B (CypB)
  • Endoplasmic reticulum
  • Lysyl hydroxylase
  • P-domain
  • Peptidyl prolyl cis-trans-isomerase (PPIase)
  • Protein complex

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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