1ule

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{{STRUCTURE_1ule| PDB=1ule | SCENE= }}
{{STRUCTURE_1ule| PDB=1ule | SCENE= }}
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'''CGL2 in complex with linear B2 trisaccharide'''
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===CGL2 in complex with linear B2 trisaccharide===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15062091 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15062091}}
==About this Structure==
==About this Structure==
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[[Category: Lectin]]
[[Category: Lectin]]
[[Category: Sugar binding]]
[[Category: Sugar binding]]
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Revision as of 00:10, 28 July 2008

Image:1ule.png

Template:STRUCTURE 1ule

CGL2 in complex with linear B2 trisaccharide

Template:ABSTRACT PUBMED 15062091

About this Structure

1ULE is a Single protein structure of sequence from Coprinopsis cinerea. Full crystallographic information is available from OCA.

Reference

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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