4AE2

Crystal structure of Human fibrillar procollagen type III C- propeptide trimer

Summary for 4AE2

• Entry DOI: 10.2210/pdb4ae2/pdb
• Related: 2V53 4AEJ 4AK3
• Descriptor: COLLAGEN ALPHA-1(III) CHAIN, CALCIUM ION, NITRATE ION, ... (4 entities in total)
• Functional Keywords: structural protein, fibrillar collagen, extracellular matrix, fibrosis
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 3
• Total formula weight: 86876.28

Authors

Bourhis, J.M.,Mariano, N.,Zhao, Y.,Harlos, K.,Jones, E.Y.,Moali, C.,Aghajari, N.,Hulmes, D.J. (deposition date: 2012-01-05, release date: 2012-09-12, Last modification date: 2024-10-23)

Primary citation

Bourhis, J.M.,Mariano, N.,Zhao, Y.,Harlos, K.,Exposito, J.Y.,Jones, E.Y.,Moali, C.,Aghajari, N.,Hulmes, D.J.
Structural Basis of Fibrillar Collagen Trimerization and Related Genetic Disorders.
Nat.Struct.Mol.Biol., 19:1031-, 2012

PubMed Abstract: 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 recognition during intracellular trimerization of the procollagen molecule. It also gives insights into why some types of collagen consist of three identical polypeptide chains, whereas others do not. Finally, the data show striking correlations between the sites of numerous disease-related mutations in different C-propeptide domains and the degree of phenotype severity. The results have broad implications for understanding genetic disorders of connective tissues and designing new therapeutic strategies.

PubMed: 23001006
DOI: 10.1038/NSMB.2389

Experimental method

X-RAY DIFFRACTION (1.68 Å)