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1ULG

CGL2 in complex with Thomsen-Friedenreich antigen

Summary for 1ULG
Entry DOI10.2210/pdb1ulg/pdb
Related1A3K 1BKZ 1C1F 1GAN 1IS5 1LCL 1QMJ 1SLA 1UL9 1ULC 1ULD 1ULE 1ULF
Descriptorgalectin-2, beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose (3 entities in total)
Functional Keywordsgalectin, lectin, beta-galactoside binding lectin, sugar binding, sugar binding protein
Biological sourceCoprinopsis cinerea
Total number of polymer chains4
Total formula weight68601.19
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 citationWalser, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

226707

數據於2024-10-30公開中

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