Structural highlights
Function
[CONA_CANEN] 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 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.
Crystal structure of the complex of concanavalin A and hexapeptide.,Zhang Z, Qian M, Huang Q, Jia Y, Tang Y, Wang K, Cui D, Li M J Protein Chem. 2001 Jul;20(5):423-9. PMID:11732694[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 hexapeptide. J Protein Chem. 2001 Jul;20(5):423-9. PMID:11732694
