| IMBERTY, Anne, Edward P. MITCHELL a Michaela WIMMEROVÁ. Structural basis of high-affinity glycan recognition by bacterial and fungal lectins. Current Opinion in Structural Biology. London: Elsevier Science Ltd., 2005, roč. 15, č. 5, s. 525-534, 11 s. ISSN 0959-440X. |
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@article{575651,
author = {Imberty, Anne and Mitchell, Edward P. and Wimmerová, Michaela},
article_location = {London},
article_number = {5},
keywords = {lectin; pathogen; crystal structure; recognition},
language = {eng},
issn = {0959-440X},
journal = {Current Opinion in Structural Biology},
title = {Structural basis of high-affinity glycan recognition by bacterial and fungal lectins},
volume = {15},
year = {2005}
}
TY - JOUR
ID - 575651
AU - Imberty, Anne - Mitchell, Edward P. - Wimmerová, Michaela
PY - 2005
TI - Structural basis of high-affinity glycan recognition by bacterial and fungal lectins
JF - Current Opinion in Structural Biology
VL - 15
IS - 5
SP - 525-534
EP - 525-534
PB - Elsevier Science Ltd.
SN - 0959440X
KW - lectin
KW - pathogen
KW - crystal structure
KW - recognition
N2 - The structural diversity of bacterial and fungal lectins has been highlighted during the past few years. Some of the new structures reproduce folds previously observed in plants or mammals, but many constitute new folds that have never been observed before, either at all or not with a lectin function, testifying to the increasing diversity. The novelty of the new structures is greater at the level of the sugar-binding sites, with some bacterial lectins displaying unusually high affinity for oligosaccharides and even monosaccharides. Analysis of the thermodynamic contributions to the energy of binding gives clues to the strategies used by bacteria to recognise and attach to their host
ER -
IMBERTY, Anne, Edward P. MITCHELL a Michaela WIMMEROVÁ. Structural basis of high-affinity glycan recognition by bacterial and fungal lectins. \textit{Current Opinion in Structural Biology}. London: Elsevier Science Ltd., 2005, roč.~15, č.~5, s.~525-534, 11 s. ISSN~0959-440X.
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