4MTY: Structure At 1a Resolution Of A Helical Aromatic Foldamer-protein Complex

Citation:
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 A resolution and revealed a number of unanticipated protein-foldamer, foldamer-foldamer, and protein-protein interactions.
PDB ID: 4MTYDownload
MMDB ID: 115912
PDB Deposition Date: 2013/9/20
Updated in MMDB: 2013/12
Experimental Method:
x-ray diffraction
Resolution: 1  Å
Source Organism:
Similar Structures:
Biological Unit for 4MTY: monomeric; determined by author and by software (PISA)
Molecular Components in 4MTY
Label Count Molecule
Protein (1 molecule)
1
Carbonic Anhydrase 2(Gene symbol: CA2)
Molecule annotation
Chemicals (10 molecules)
1
1
2
3
3
1
4
4
5
1
* Click molecule labels to explore molecular sequence information.

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