6SYJ

Crystal structure of a ProM2 containing triple-helical collagen peptide.

6SYJ の概要

• エントリーDOI: 10.2210/pdb6syj/pdb
• 分子名称: ProM2 containing collagen model peptide. (2 entities in total)
• 機能のキーワード: collagen model peptide, protein engineering, collagen stability, structural protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 8676.74

構造登録者

Gebauer, J.M.,Maassen, A.,Schmalz, H.-G.,Baumann, U. (登録日: 2019-09-30, 公開日: 2020-01-29, 最終更新日: 2024-10-09)

主引用文献

Maassen, A.,Gebauer, J.M.,Theres Abraham, E.,Grimm, I.,Neudorfl, J.M.,Kuhne, R.,Neundorf, I.,Baumann, U.,Schmalz, H.G.
Triple-Helix-Stabilizing Effects in Collagen Model Peptides Containing PPII-Helix-Preorganized Diproline Modules.
Angew.Chem.Int.Ed.Engl., 59:5747-5755, 2020

PubMed Abstract: Collagen model peptides (CMPs) serve as tools for understanding stability and function of the collagen triple helix and have a potential for biomedical applications. In the past, interstrand cross-linking or conformational preconditioning of proline units through stereoelectronic effects have been utilized in the design of stabilized CMPs. To further study the effects determining collagen triple helix stability we investigated a series of CMPs containing synthetic diproline-mimicking modules (ProMs), which were preorganized in a PPII-helix-type conformation by a functionalizable intrastrand C bridge. Results of CD-based denaturation studies were correlated with calculated (DFT) conformational preferences of the ProM units, revealing that the relative helix stability is mainly governed by an interplay of main-chain preorganization, ring-flip preference, adaptability, and steric effects. Triple helix integrity was proven by crystal structure analysis and binding to HSP47.

PubMed: 31944532
DOI: 10.1002/anie.201914101

実験手法

X-RAY DIFFRACTION (0.81 Å)