
doi: 10.1038/306447a0
pmid: 6646225
The crystal structure of leucine-enkephalin has been determined in a crystal form that has four independent enkephalin molecules and much water and dimethylformamide solvent in the asymmetric unit. All four enkephalins have extended peptide backbones with the Tyr, Phe and Leu side chains above and below the plane of the backbone. There is evidence that this extended conformation may provide an acceptable model for enkephalin binding to opiate mu-receptors.
Models, Molecular, Structure-Activity Relationship, Crystallography, X-Ray Diffraction, Protein Conformation, Enkephalin, Leucine
Models, Molecular, Structure-Activity Relationship, Crystallography, X-Ray Diffraction, Protein Conformation, Enkephalin, Leucine
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