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2cy6

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(New page: 200px<br /><applet load="2cy6" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cy6, resolution 2.00&Aring;" /> '''Crystal structure of...)
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Revision as of 07:13, 21 November 2007

Image:2cy6.gif

2cy6, resolution 2.00Å

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Crystal structure of ConM in complex with trehalose and maltose

Overview

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.

About this Structure

2CY6 is a Protein complex structure of sequences from Canavalia maritima with CA, MN and TRE as ligands. 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

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