6SYJ

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

Summary for 6SYJ

• Entry DOI: 10.2210/pdb6syj/pdb
• Descriptor: ProM2 containing collagen model peptide. (2 entities in total)
• Functional Keywords: collagen model peptide, protein engineering, collagen stability, structural protein
• Biological source: synthetic construct
• Total number of polymer chains: 3
• Total formula weight: 8676.74

Authors

Gebauer, J.M.,Maassen, A.,Schmalz, H.-G.,Baumann, U. (deposition date: 2019-09-30, release date: 2020-01-29, Last modification date: 2024-10-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (0.81 Å)