The Binding of Human Carbonic Anhydrase II by Functionalized Folded Polypeptide Receptors
| Autor: | Lars Baltzer, Theresa Andersson, Bengt-Harald Jonsson, Karin Enander, Jonas Nilsson, Martin Lundquist, Gunnar T. Dolphin |
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| Rok vydání: | 2005 |
| Předmět: |
Models
Molecular Pharmacology Protein Folding Binding Sites Magnetic Resonance Spectroscopy genetic structures Sequence Homology Amino Acid Carbonic anhydrase II Molecular Sequence Data Clinical Biochemistry Cooperative binding General Medicine Biology Carbonic Anhydrase II Biochemistry Protein Structure Tertiary Drug Discovery Humans Molecular Medicine Amino Acid Sequence Receptor Peptides Molecular Biology Protein Binding |
| Zdroj: | Chemistry & Biology. 12(11):1245-1252 |
| ISSN: | 1074-5521 |
| DOI: | 10.1016/j.chembiol.2005.08.018 |
| Popis: | SummarySeveral receptors for human carbonic anhydrase II (HCAII) have been prepared by covalently attaching benzenesulfonamide carboxylates via aliphatic aminocarboxylic acid spacers of variable length to the side chain of a lysine residue in a designed 42 residue helix-loop-helix motif. The sulfonamide group binds to the active site zinc ion of human carbonic anhydrase II located in a 15 Å deep cleft. The dissociation constants of the receptor-HCAII complexes were found to be in the range from low micromolar to better than 20 nM, with the lowest affinities found for spacers with less than five methylene groups and the highest affinity found for the spacer with seven methylene groups. The results suggest that the binding is a cooperative event in which both the sulfonamide residue and the helix-loop-helix motif contribute to the overall affinity. |
| Databáze: | OpenAIRE |
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