6OLN
Controlling the Self-Assembly of Synthetic Metal-Coordinating Coiled-Coil Peptides: Orthorhombic Lattice from a Trimeric Coiled Coil
Summary for 6OLN
Entry DOI | 10.2210/pdb6oln/pdb |
Descriptor | Designed trimeric coiled coil peptide, COPPER (II) ION, CHLORIDE ION, ... (4 entities in total) |
Functional Keywords | de novo protein, metal coordination framework, supramolecular assembly |
Biological source | synthetic construct |
Total number of polymer chains | 6 |
Total formula weight | 19648.99 |
Authors | Scheib, K.A.,Horne, W.S. (deposition date: 2019-04-16, release date: 2020-02-19, Last modification date: 2023-11-15) |
Primary citation | Scheib, K.A.,Tavenor, N.A.,Lawless, M.J.,Saxena, S.,Horne, W.S. Understanding and controlling the metal-directed assembly of terpyridine-functionalized coiled-coil peptides. Chem.Commun.(Camb.), 55:7752-7755, 2019 Cited by PubMed Abstract: Metal-binding peptides are versatile building blocks in supramolecular chemistry. We recently reported a class of crystalline materials formed through a combination of coiled-coil peptide self-association and metal coordination. Here, we probe the serendipitously discovered metal binding motif that drives the assembly and apply these insights to exert rational control over structure and morphology in the materials. PubMed: 31204733DOI: 10.1039/c9cc03496j PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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