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| - | [[Image:2r0h.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2r0h| PDB=2r0h | SCENE= }} | | {{STRUCTURE_2r0h| PDB=2r0h | SCENE= }} |
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| - | '''Fungal lectin CGL3 in complex with chitotriose (chitotetraose)'''
| + | ===Fungal lectin CGL3 in complex with chitotriose (chitotetraose)=== |
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| - | ==Overview==
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| - | Recent advances in genome sequencing efforts have revealed an abundance of novel putative lectins. Among these, many galectin-related proteins, characterized by many conserved residues but intriguingly lacking critical amino acids, have been found in all corners of the eukaryotic superkingdom. Here we present a structural and biochemical analysis of one representative, the galectin-related lectin CGL3 found in the inky cap mushroom Coprinopsis cinerea. This protein contains all but one conserved residues known to be involved in beta-galactoside binding in galectins. A Trp residue strictly conserved among galectins is changed to an Arg in CGL3 (R81). Accordingly, the galectin-related protein is not able to bind lactose. Screening of a glycan array revealed that CGL3 displays preference for oligomers of beta1-4-linked N-acetyl-glucosamines (chitooligosaccharides) and GalNAc beta 1-4GlcNAc (LacdiNAc). Carbohydrate-binding affinity of this novel lectin was quantified using isothermal titration calorimetry, and its mode of chitooligosaccharide coordination not involving any aromatic amino acid residues was studied by X-ray crystallography. Structural information was used to alter the carbohydrate-binding specificity and substrate affinity of CGL3. The importance of residue R81 in determining the carbohydrate-binding specificity was demonstrated by replacing this Arg with a Trp residue (R81W). This single-amino-acid change led to a lectin that failed to bind chitooligosaccharides but gained lactose binding. Our results demonstrate that, similar to the legume lectin fold, the galectin fold represents a conserved structural framework upon which dramatically altered specificities can be grafted by few alterations in the binding site and that, in consequence, many metazoan galectin-related proteins may represent lectins with novel carbohydrate-binding specificities.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_18440554}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 18440554 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_18440554}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Lectin]] | | [[Category: Lectin]] |
| | [[Category: Sugar binding protein]] | | [[Category: Sugar binding protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 21:37:12 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:13:04 2008'' |
Revision as of 20:13, 28 July 2008
Template:STRUCTURE 2r0h
Fungal lectin CGL3 in complex with chitotriose (chitotetraose)
Template:ABSTRACT PUBMED 18440554
About this Structure
2R0H is a Single protein structure of sequence from Coprinopsis cinerea. Full crystallographic information is available from OCA.
Reference
Structural basis for chitotetraose coordination by CGL3, a novel galectin-related protein from Coprinopsis cinerea., Walti MA, Walser PJ, Thore S, Grunler A, Bednar M, Kunzler M, Aebi M, J Mol Biol. 2008 May 23;379(1):146-59. Epub 2008 Apr 3. PMID:18440554
Page seeded by OCA on Mon Jul 28 23:13:04 2008
