1ULD

CGL2 in complex with blood group H type II

Summary for 1ULD

• Entry DOI: 10.2210/pdb1uld/pdb
• Related: 1A3K 1BKZ 1C1F 1GAN 1IS5 1LCL 1QMJ 1SLA 1UL9 1ULC 1ULE 1ULF 1ULG
• Related PRD ID: PRD_900036
• Descriptor: galectin-2, alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: galectin, lectin, beta-galactoside binding lectin, sugar binding, sugar binding protein
• Biological source: Coprinopsis cinerea
• Total number of polymer chains: 4
• Total formula weight: 69185.76

Authors

Walser, P.J.,Haebel, P.W.,Kuenzler, M.,Kues, U.,Aebi, M.,Ban, N. (deposition date: 2003-09-12, release date: 2004-04-20, Last modification date: 2024-04-03)

Primary citation

Walser, P.J.,Haebel, P.W.,Kuenzler, M.,Sargent, D.,Kues, U.,Aebi, M.,Ban, N.
Structure and Functional Analysis of the Fungal Galectin CGL2
STRUCTURE, 12:689-702, 2004

PubMed Abstract: Recognition of and discrimination between potential glyco-substrates is central to the function of galectins. Here we dissect the fundamental parameters responsible for such selectivity by the fungal representative, CGL2. The 2.1 A crystal structure of CGL2 and five substrate complexes reveal that this prototype galectin achieves increased substrate specificity by accommodating substituted oligosaccharides of the mammalian blood group A/B type in an extended binding cleft. Kinetic studies on wild-type and mutant CGL2 proteins demonstrate that the tetrameric organization is essential for functionality. The geometric constraints due to the orthogonal orientation of the four binding sites have important consequences on substrate binding and selectivity.

PubMed: 15062091
DOI: 10.1016/j.str.2004.03.002

Experimental method

X-RAY DIFFRACTION (2.1 Å)