Structural basis of fibrillar collagen trimerization and related genetic disorders.

Journal article

The C propeptides of fibrillar procollagens have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. Mutations in C propeptides are associated with several, often lethal, genetic disorders affecting bone, cartilage, blood vessels and skin. Here we report the crystal structure of a C-propeptide domain from human procollagen III. It reveals an exquisite structural mechanism of chain...

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Authors: Bourhis, J; Mariano, N; Zhao, Y; Harlos, K; Exposito, J

• Publication status: Published
• Journal: Nature structural and molecular biology
• Volume: 19
• Issue: 10
• Pages: 1031-1036
• Publication date: 2012-10-01
• DOI: 10.1038/nsmb.2389
• EISSN: 1545-9985
• ISSN: 1545-9993
• Language: English
• Keywords: Collagen Diseases; Models, Molecular; Crystallography, X-Ray; Protein Multimerization; Collagen Type III; Amino Acid Sequence; Molecular Sequence Data; Mutation, Missense; Mutation; Humans; Protein Structure, Tertiary