1CAG

CRYSTAL AND MOLECULAR STRUCTURE OF A COLLAGEN-LIKE PEPTIDE AT 1.9 ANGSTROM RESOLUTION

1CAG の概要

• エントリーDOI: 10.2210/pdb1cag/pdb
• 分子名称: COLLAGEN-LIKE PEPTIDE, ACETIC ACID (3 entities in total)
• 機能のキーワード: collagen
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 8474.87

構造登録者

Bella, J.,Eaton, M.,Brodsky, B.,Berman, H.M. (登録日: 1994-03-29, 公開日: 1994-11-01, 最終更新日: 2024-06-05)

主引用文献

Bella, J.,Eaton, M.,Brodsky, B.,Berman, H.M.
Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution.
Science, 266:75-81, 1994

PubMed Abstract: The structure of a protein triple helix has been determined at 1.9 angstrom resolution by x-ray crystallographic studies of a collagen-like peptide containing a single substitution of the consensus sequence. This peptide adopts a triple-helical structure that confirms the basic features determined from fiber diffraction studies on collagen: supercoiling of polyproline II helices and interchain hydrogen bonding that follows the model II of Rich and Crick. In addition, the structure provides new information concerning the nature of this protein fold. Each triple helix is surrounded by a cylinder of hydration, with an extensive hydrogen bonding network between water molecules and peptide acceptor groups. Hydroxyproline residues have a critical role in this water network. The interaxial spacing of triple helices in the crystal is similar to that in collagen fibrils, and the water networks linking adjacent triple helices in the crystal structure are likely to be present in connective tissues. The breaking of the repeating (X-Y-Gly)n pattern by a Gly-->Ala substitution results in a subtle alteration of the conformation, with a local untwisting of the triple helix. At the substitution site, direct interchain hydrogen bonds are replaced with interstitial water bridges between the peptide groups. Similar conformational changes may occur in Gly-->X mutated collagens responsible for the diseases osteogenesis imperfecta, chondrodysplasias, and Ehlers-Danlos syndrome IV.

PubMed: 7695699

実験手法

X-RAY DIFFRACTION (1.85 Å)