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2cy6

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{{STRUCTURE_2cy6| PDB=2cy6 | SCENE= }}
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'''Crystal structure of ConM in complex with trehalose and maltose'''
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===Crystal structure of ConM in complex with trehalose and maltose===
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==Overview==
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The crystal structure of Canavalia maritima lectin (ConM) complexed with trehalose and maltose revealed relevant point mutations in ConA-like lectins. ConM with the disaccharides and other ConA-like lectins complexed with carbohydrates demonstrated significant differences in the position of H-bonds. The main difference in the ConM structure is the replacement of Pro202 by Ser202, a residue that promotes the approximation of Tyr12 to the carbohydrate-binding site. The O-6' of the second glucose ring in maltose interacts with Tyr12, while in trehalose the interaction is established by the O-2' and Tyr12, explaining the higher affinity of ConM for disaccharides compared to monosaccharides.
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{{ABSTRACT_PUBMED_16677825}}
==About this Structure==
==About this Structure==
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[[Category: Trehalose]]
[[Category: Trehalose]]
[[Category: X-ray diffraction]]
[[Category: X-ray diffraction]]
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Revision as of 20:33, 28 July 2008

Image:2cy6.png

Template:STRUCTURE 2cy6

Crystal structure of ConM in complex with trehalose and maltose

Template:ABSTRACT PUBMED 16677825

About this Structure

Full crystallographic information is available from OCA.

Reference

Crystal structure of a lectin from Canavalia maritima (ConM) in complex with trehalose and maltose reveals relevant mutation in ConA-like lectins., Delatorre P, Rocha BA, Gadelha CA, Santi-Gadelha T, Cajazeiras JB, Souza EP, Nascimento KS, Freire VN, Sampaio AH, Azevedo WF Jr, Cavada BS, J Struct Biol. 2006 Jun;154(3):280-6. Epub 2006 Apr 21. PMID:16677825

Page seeded by OCA on Mon Jul 28 23:33:24 2008

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