Structural highlights
Function
[CONA_CANCT] Glucose/D-mannose specific lectin.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The X-ray structure analysis of a cross-linked crystal of concanavalin A soaked with the tripeptide molecule as the probe molecule showed 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 tripeptide complex was refined at 2.4-A resolution to an R-factor of 17.5%, (Rfree factor of 23.7%), with an RMS deviation in bond distances of 0.01 A. The model includes all 237 residue of concanavalin A, 1 manganese ion, 1 calcium ion, 161 water molecules, 1 glutaraldehyde molecule, and 1 tripeptide 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 a mixture of organic solvent with water or in neat organic solvent but is hardly dissolved in aqueous solution.
Crystal structure of the complex of concanavalin A and tripeptide.,Zhang Z, Qian M, Huang Q, Jia Y, Tang Y, Wang K, Cui D, Li M J Protein Chem. 2001 Jan;20(1):59-65. PMID:11330349[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhang Z, Qian M, Huang Q, Jia Y, Tang Y, Wang K, Cui D, Li M. Crystal structure of the complex of concanavalin A and tripeptide. J Protein Chem. 2001 Jan;20(1):59-65. PMID:11330349
