4K20: Crystal Structure Of Canavalia Boliviana Lectin

Plant lectins, especially those purified from species of the Leguminosae family, represent the best-studied group of carbohydrate-binding proteins. Lectins purified from seeds of the Diocleinae subtribe exhibit a high degree of sequence identity notwithstanding that they show very distinct biological activities. Two main factors have been related to this feature: variance in key residues influencing the carbohydrate-binding site geometry and differences in the pH-dependent oligomeric state profile. In this work, we have isolated a lectin from Canavalia boliviana (Cbol) and solved its x-ray crystal structure in the unbound form and in complex with the carbohydrates Man(alpha1-3)Man(alpha1-O)Me, Man(alpha1-4)Man(alpha1-O)Me and 5-bromo-4-chloro-3-indolyl-alpha-D-mannose. We evaluated its oligomerization profile at different pH values using Small Angle X-ray Scattering and compared it to that of Concanavalin A. Based on predicted pKa-shifts of amino acids in the subunit interfaces we devised a model for the dimer-tetramer equilibrium phenomena of these proteins. Additionally, we demonstrated Cbol anti-inflammatory properties and further characterized them using in vivo and in vitro models.
PDB ID: 4K20Download
MMDB ID: 119009
PDB Deposition Date: 2013/4/7
Updated in MMDB: 2014/06
Experimental Method:
x-ray diffraction
Resolution: 3.4  Å
Source Organism:
Similar Structures:
Biological Unit for 4K20: tetrameric; determined by author and by software (PISA)
Molecular Components in 4K20
Label Count Molecule
Proteins (4 molecules)
Canavalia Boliviana Lectin
Molecule annotation
Chemicals (8 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB