7JX5
Crystal Structure of N-Phenylalanine Peptoid-modified Collagen Triple Helix
Summary for 7JX5
| Entry DOI | 10.2210/pdb7jx5/pdb |
| Related | 7JX4 |
| Descriptor | Collagen mimetic peptide with N-Phenylalanine guest (2 entities in total) |
| Functional Keywords | collagen, peptoid, triple helix, hyper-stable, protein fibril |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 6 |
| Total formula weight | 11778.53 |
| Authors | Yu, M.S.,Whitby, F.G.,Hill, C.P.,Kessler, J.L.,Yang, L.D. (deposition date: 2020-08-26, release date: 2021-07-21, Last modification date: 2023-11-15) |
| Primary citation | Kessler, J.L.,Kang, G.,Qin, Z.,Kang, H.,Whitby, F.G.,Cheatham, T.E.,Hill, C.P.,Li, Y.,Yu, S.M. Peptoid Residues Make Diverse, Hyperstable Collagen Triple-Helices J.Am.Chem.Soc., 143:10910-10919, 2021 Cited by PubMed Abstract: As the only ribosomally encoded N-substituted amino acid, proline promotes distinct secondary protein structures. The high proline content in collagen, the most abundant protein in the human body, is crucial to forming its hallmark structure: the triple-helix. For over five decades, proline has been considered compulsory for synthetic designs aimed at recapitulating collagen's structure and properties. Here we describe that N-substituted glycines (N-glys), also known as peptoid residues, exhibit a general triple-helical propensity similar to or greater than proline, enabling synthesis of stable triple-helical collagen mimetic peptides (CMPs) with unprecedented side chain diversity. Supported by atomic-resolution crystal structures as well as circular dichroism and computational characterizations spanning over 30 N-gly-containing CMPs, we discovered that N-glys stabilize the triple-helix primarily by sterically preorganizing individual chains into the polyproline-II helix. We demonstrated that N-glys with exotic side chains including a "click"-able alkyne and a photosensitive side chain enable CMPs for functional applications including the spatiotemporal control of cell adhesion and migration. The structural principles uncovered in this study open up opportunities for a new generation of collagen-mimetic therapeutics and materials. PubMed: 34255504DOI: 10.1021/jacs.1c00708 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.1 Å) |
Structure validation
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