X-ray studies on ligands.
Advances in x-ray crystallographic data collection, structure solution, and refinement/validation have reduced the time required and expanded the range of samples amenable to x-ray crystallographic studies. Consequently, we can now collect complete atomic resolution data sets on physically smaller crystals and solve larger problems by direct methods beyond what could have been accomplished even five years ago. Applying these improved methods to the study of opioid ligands has enhanced our knowledge of the opioid pharmacophore. Despite considerable progress, it is still difficult to define the pharmacophoric parameters required for highly selective and potent opioid peptides. In part this is due to the conformational flexibility remaining even in conformationally constrained peptides.
Deschamps
Jeffrey R
JR
Laboratory for the Structure of Matter, Naval Research Laboratory Washington, DC 20375, USA. deschamps@nrl.navy.mil
Flippen-Anderson
Judith L
JL
George
Clifford
C
D018360:Crystallography, X-Ray / Q000379:methods; D004151:Dipeptides / Q000737:chemistry; D004745:Enkephalins / Q000737:chemistry; D008024:Ligands; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D012680:Sensitivity and Specificity
D004151:Dipeptides; D004745:Enkephalins; D008024:Ligands; D010455:Peptides