| BONNARDEL, Francois, Atul KUMAR, Michaela WIMMEROVÁ, Martina LAHMANN, Serge PEREZ, Annabelle VARROT, Frederique LISACEK a Anne IMBERTY. Architecture and Evolution of Blade Assembly in beta-propeller Lectins. Structure. CAMBRIDGE: CELL PRESS, 2019, roč. 27, č. 5, s. 764-775. ISSN 0969-2126. Dostupné z: https://dx.doi.org/10.1016/j.str.2019.02.002. |
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@article{1608896,
author = {Bonnardel, Francois and Kumar, Atul and Wimmerová, Michaela and Lahmann, Martina and Perez, Serge and Varrot, Annabelle and Lisacek, Frederique and Imberty, Anne},
article_location = {CAMBRIDGE},
article_number = {5},
doi = {http://dx.doi.org/10.1016/j.str.2019.02.002},
keywords = {lectin; beta-propellers},
language = {eng},
issn = {0969-2126},
journal = {Structure},
title = {Architecture and Evolution of Blade Assembly in beta-propeller Lectins},
url = {https://www.sciencedirect.com/science/article/abs/pii/S0969212619300462?via%3Dihub},
volume = {27},
year = {2019}
}
TY - JOUR
ID - 1608896
AU - Bonnardel, Francois - Kumar, Atul - Wimmerová, Michaela - Lahmann, Martina - Perez, Serge - Varrot, Annabelle - Lisacek, Frederique - Imberty, Anne
PY - 2019
TI - Architecture and Evolution of Blade Assembly in beta-propeller Lectins
JF - Structure
VL - 27
IS - 5
SP - 764-775
EP - 764-775
PB - CELL PRESS
SN - 09692126
KW - lectin
KW - beta-propellers
UR - https://www.sciencedirect.com/science/article/abs/pii/S0969212619300462?via%3Dihub
L2 - https://www.sciencedirect.com/science/article/abs/pii/S0969212619300462?via%3Dihub
N2 - Lectins with a beta-propeller fold bind glycans on the cell surface through multivalent binding sites and appropriate directionality. These proteins are formed by repeats of short domains, raising questions about evolutionary duplication. However, these repeats are difficult to detect in translated genomes and seldom correctly annotated in sequence databases. To address these issues, we defined the blade signature of the five types of beta-propellers using 3D-structural data. With these templates, we predicted 3,887 beta-propeller lectins in 1,889 species and organized this information in a searchable online database. The data reveal a widespread distribution of beta-propeller lectins across species. Prediction also emphasizes multiple architectures and led to the discovery of a beta-propeller assembly scenario. This was confirmed by producing and characterizing a predicted protein coded in the genome of Kordia zhangzhouensis. The crystal structure uncovers an intermediate in the evolution of beta-propeller assembly and demonstrates the power of our tools.
ER -
BONNARDEL, Francois, Atul KUMAR, Michaela WIMMEROVÁ, Martina LAHMANN, Serge PEREZ, Annabelle VARROT, Frederique LISACEK a Anne IMBERTY. Architecture and Evolution of Blade Assembly in beta-propeller Lectins. \textit{Structure}. CAMBRIDGE: CELL PRESS, 2019, roč.~27, č.~5, s.~764-775. ISSN~0969-2126. Dostupné z: https://dx.doi.org/10.1016/j.str.2019.02.002.
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