4MTY

Structure at 1A resolution of a helical aromatic foldamer-protein complex.

Summary for 4MTY

• Entry DOI: 10.2210/pdb4mty/pdb
• Descriptor: Carbonic anhydrase 2, ZINC ION, N-(3-hydroxybenzyl)-4-sulfamoylbenzamide, ... (7 entities in total)
• Functional Keywords: mixed alpha beta, lyase-lyase inhibitor complex, lyase/lyase inhibitor
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : P00918
• Total number of polymer chains: 1
• Total formula weight: 31181.16

Authors

Ogayone, T.,Buratto, J.,Langlois D'Estaintot, B.,Stupfel, M.,Granier, T.,Gallois, B.,Huc, Y. (deposition date: 2013-09-20, release date: 2013-12-11, Last modification date: 2023-09-20)

Primary citation

Buratto, J.,Colombo, C.,Stupfel, M.,Dawson, S.J.,Dolain, C.,Langlois d'Estaintot, B.,Fischer, L.,Granier, T.,Laguerre, M.,Gallois, B.,Huc, I.
Structure of a complex formed by a protein and a helical aromatic oligoamide foldamer at 2.1 a resolution.
Angew.Chem.Int.Ed.Engl., 53:883-887, 2014

PubMed Abstract: In the search of molecules that could recognize sizeable areas of protein surfaces, a series of ten helical aromatic oligoamide foldamers was synthesized on solid phase. The foldamers comprise three to five monomers carrying various proteinogenic side chains, and exist as racemic mixtures of interconverting right-handed and left-handed helices. Functionalization of the foldamers by a nanomolar ligand of human carbonic anhydrase II (HCA) ensured that they would be held in close proximity to the protein surface. Foldamer-protein interactions were screened by circular dichroism (CD). One foldamer displayed intense CD bands indicating that a preferred helix handedness is induced upon interacting with the protein surface. The crystal structure of the complex between this foldamer and HCA could be resolved at 2.1 Å resolution and revealed a number of unanticipated protein-foldamer, foldamer-foldamer, and protein-protein interactions.

PubMed: 24288253
DOI: 10.1002/anie.201309160

Experimental method

X-RAY DIFFRACTION (1 Å)