2cyf
From Proteopedia
|
The Crystal Structure of Canavalia Maritima Lectin (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
2CYF is a Protein complex structure of sequences from Canavalia maritima with MAL, CA and MN 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
Page seeded by OCA on Wed Nov 21 09:20:43 2007
