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, B├Ąchinger HP
BMC Res Notes. 2012 5: 626

PMID: 23137129 · PMCID: PMC3522003 · DOI:10.1186/1756-0500-5-626

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.

MeSH Terms (11)

Animals Crystallography, X-Ray Cyclophilins Horse Diseases Horses Models, Molecular Mutation, Missense Protein Structure, Secondary Protein Structure, Tertiary Skin Skin Diseases

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