%0 Journal Article %1 WOS:000238104900007 %A Delatorre, Plinio %A Rocha, Bruno A M %A Gadelha, Carlos A A %A Santi-Gadelha, Tatiane %A Cajazeiras, Joao B %A Souza, Emmanuel P %A Nascimento, Kyria S %A Freire, Valder N %A Sampaio, Alexandre H %A Jr., Walter F Azevedo %A Cavada, Benildo S %C 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA %D 2006 %I ACADEMIC PRESS INC ELSEVIER SCIENCE %J JOURNAL OF STRUCTURAL BIOLOGY %K Canavalia crystal maritima; mutation} structure; {lectins; %N 3 %P 280-286 %R 10.1016/j.jsb.2006.03.011 %T Crystal structure of a lectin from Canavalia maritima (ConM) in complex with trehalose and maltose reveals relevant. mutation in ConA-like lectins %V 154 %X 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. (c) 2006 Elsevier Inc. All rights reserved.

@article{WOS:000238104900007, abstract = {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. (c) 2006 Elsevier Inc. All rights reserved.}, added-at = {2022-05-23T20:00:14.000+0200}, address = {525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA}, author = {Delatorre, Plinio and Rocha, Bruno A M and Gadelha, Carlos A A and Santi-Gadelha, Tatiane and Cajazeiras, Joao B and Souza, Emmanuel P and Nascimento, Kyria S and Freire, Valder N and Sampaio, Alexandre H and Jr., Walter F Azevedo and Cavada, Benildo S}, biburl = {https://www.bibsonomy.org/bibtex/2d23f84106cd4074e7e4ca7bd426a7d0f/ppgfis_ufc_br}, doi = {10.1016/j.jsb.2006.03.011}, interhash = {089607e5cb7ea820971e4b3842c19d3b}, intrahash = {d23f84106cd4074e7e4ca7bd426a7d0f}, issn = {1047-8477}, journal = {JOURNAL OF STRUCTURAL BIOLOGY}, keywords = {Canavalia crystal maritima; mutation} structure; {lectins;}, number = 3, pages = {280-286}, publisher = {ACADEMIC PRESS INC ELSEVIER SCIENCE}, pubstate = {published}, timestamp = {2022-05-23T20:00:14.000+0200}, title = {Crystal structure of a lectin from Canavalia maritima (ConM) in complex with trehalose and maltose reveals relevant. mutation in ConA-like lectins}, tppubtype = {article}, volume = 154, year = 2006 }