Summary for 6HZX
| Entry DOI | 10.2210/pdb6hzx/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, quinoline oligoamide foldamer, benzene sulfonamide modified inhibitor, lyase-lyase inhibitor complex, lyase |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 6 |
| Total formula weight | 67217.17 |
| Authors | Post, S.,Langlois d'Estaintot, B.,Fischer, L.,Granier, T.,Huc, I. (deposition date: 2018-10-24, release date: 2019-09-18, Last modification date: 2024-08-14) |
| Primary citation | Reddy, P.S.,Langlois d'Estaintot, B.,Granier, T.,Mackereth, C.D.,Fischer, L.,Huc, I. Structure Elucidation of Helical Aromatic Foldamer-Protein Complexes with Large Contact Surface Areas. Chemistry, 25:11042-11047, 2019 Cited by PubMed Abstract: The development of large synthetic ligands could be useful to target the sizeable surface areas involved in protein-protein interactions. Herein, we present long helical aromatic oligoamide foldamers bearing proteinogenic side chains that cover up to 450 Å of the human carbonic anhydrase II (HCA) surface. The foldamers are composed of aminoquinolinecarboxylic acids bearing proteinogenic side chains and of more flexible aminomethyl-pyridinecarboxylic acids that enhance helix handedness dynamics. Crystal structures of HCA-foldamer complexes were obtained with a 9- and a 14-mer both showing extensive protein-foldamer hydrophobic contacts. In addition, foldamer-foldamer interactions seem to be prevalent in the crystal packing, leading to the peculiar formation of an HCA superhelix wound around a rod of stacked foldamers. Solution studies confirm the positioning of the foldamer at the protein surface as well as a dimerization of the complexes. PubMed: 31257622DOI: 10.1002/chem.201902942 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.91 Å) |
Structure validation
Download full validation report
