5L3O
Crystal Structure of Human Carbonic Anhydrase II in Complex with a Quinoline Oligoamide Foldamer
This is a non-PDB format compatible entry.
Summary for 5L3O
| Entry DOI | 10.2210/pdb5l3o/pdb |
| Descriptor | Carbonic anhydrase 2, Aromatic foldamer, ZINC ION, ... (5 entities in total) |
| Functional Keywords | protein-foldamer complex, protein foldamer interactions, modified inhibitor, anchored foldamer, hcaii dimerisation, quinoline oligoamide foldamer, benzene sulfonamide modified inhibitor, lyase-inhibitor complex, lyase/inhibitor |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 6 |
| Total formula weight | 64703.08 |
| Authors | Jewginski, M.,Langlois d'Estaintot, B.,Granier, T.,Huc, Y. (deposition date: 2016-05-24, release date: 2017-03-01, Last modification date: 2024-09-04) |
| Primary citation | Jewginski, M.,Granier, T.,Langlois d'Estaintot, B.,Fischer, L.,Mackereth, C.D.,Huc, I. Self-Assembled Protein-Aromatic Foldamer Complexes with 2:3 and 2:2:1 Stoichiometries. J. Am. Chem. Soc., 139:2928-2931, 2017 Cited by PubMed Abstract: The promotion of protein dimerization using the aggregation properties of a protein ligand was explored and shown to produce complexes with unusual stoichiometries. Helical foldamer 2 was synthesized and bound to human carbonic anhydrase (HCA) using a nanomolar active site ligand. Crystal structures show that the hydrophobicity of 2 and interactions of its side chains lead to the formation of an HCA-2 complex in which three helices of 2 are stacked, two of them being linked to an HCA molecule. The middle foldamer in the stack can be replaced by alternate sequences 3 or 5. Solution studies by CD and NMR confirm left-handedness of the helical foldamers as well as HCA dimerization. PubMed: 28170240DOI: 10.1021/jacs.7b00184 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.98 Å) |
Structure validation
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