Crystal structure of the complex of concanavalin A and hexapeptide.
The X-ray structure analysis of a cross-linked crystal of concanavalin A soaked with a hexapeptide molecule as a probe molecule showed an electron density corresponding to full occupation in the binding pocket. The site lies on the surface of concanavalin A and is surrounded by three symmetry-related molecules. The crystal structure of the hexapeptide complex was refined at 1.93-A resolution, to an R-factor of 19% (Rfree factor of 25%), with an RMS deviation in bond distances of 0.01 A. The model includes all 237 residues of concanavalin A, one manganese ion, one calcium ion, 95 water molecules, one glutaraldehyde molecule, one isopropanol molecule, and one hexapeptide molecule. This X-ray structure analysis also provides an approach to mapping the binding surface of crystalline protein with a probe molecule that is dissolved in the mixture of organic solvent with water or in neat organic solvent but is hardly dissolved in aqueous solution.
Zhang
Z
Z
Department of Chemistry, Peking University, Beijing, China.
Qian
M
M
Huang
Q
Q
Jia
Y
Y
Tang
Y
Y
Wang
K
K
Cui
D
D
Li
M
M
D001665:Binding Sites; D003208:Concanavalin A / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry*; D025941:Protein Interaction Mapping
D009842:Oligopeptides; D003208:Concanavalin A