Publication | Closed Access
A Designed Non‐Peptidic Receptor that Mimics the Phosphocholine Binding Site of the McPC603 Antibody
56
Citations
23
References
1996
Year
Proteinlipid InteractionMolecular BiologyPeptide ScienceMolecular PharmacologyAmmonium GroupMcpc603 AntibodyNon‐peptidic ReceptorBiochemistryReceptor (Biochemistry)Biochemical InteractionNon-peptide LigandPharmacologyAntibody Mcpc603Molecular ModelingProtein PhosphorylationSignal TransductionCholine PhosphateNatural SciencesCellular BiochemistryMedicinePhosphocholine Binding Site
The two key interactions in the binding of phosphorylcholine by the antibody McPC603 are utilized in the complexation of dioctanoyl-L-α-phosphatidyl-choline (DOPC) and a novel non-peptidic abiotic receptor. These interactions are drawn as dotted lines in the structure of the complex shown on the right: hydrogen bonds between the choline phosphate and the guanidinium unit of the receptor, and cation–π interactions between the ammonium group of DOPC and the calixarene unit of the receptor.
| Year | Citations | |
|---|---|---|
Page 1
Page 1