4AEJ

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

4AEJ の概要

• エントリーDOI: 10.2210/pdb4aej/pdb
• 関連するPDBエントリー: 2V53 4AE2 4AK3
• 分子名称: COLLAGEN ALPHA-1(III) CHAIN, CALCIUM ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: structural protein, extracellular, matrix, fibrosis, trimer
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 88055.01

構造登録者

Bourhis, J.M.,Mariano, N.,Zhao, Y.,Harlos, K.,Jones, E.Y.,Moali, C.,Aghajari, N.,Hulmes, D.J.S. (登録日: 2012-01-11, 公開日: 2012-09-12, 最終更新日: 2024-10-09)

主引用文献

Bourhis, J.M.,Mariano, N.,Zhao, Y.,Harlos, K.,Exposito, J.,Jones, E.Y.,Moali, C.,Aghajari, N.,Hulmes, D.J.S.
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

実験手法

X-RAY DIFFRACTION (2.21 Å)