1ulf
CGL2 in complex with Blood Group A tetrasaccharide
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OverviewOverview
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.
About this StructureAbout this Structure
1ULF is a Single protein structure of sequence from Coprinopsis cinerea. Full crystallographic information is available from OCA.
ReferenceReference
Structure and functional analysis of the fungal galectin CGL2., Walser PJ, Haebel PW, Kunzler M, Sargent D, Kues U, Aebi M, Ban N, Structure. 2004 Apr;12(4):689-702. PMID:15062091
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