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Interactions between a Heparin Trisaccharide Library and FGF-1 Analyzed by NMR Methods

Opened Access Interactions between a Heparin Trisaccharide Library and FGF-1 Analyzed by NMR Methods

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Autor: García Jiménez, María
Gil Caballero, Sergio
Nieto Mesa, Pedro Manuel
Canales, Ángeles
Jiménez Barbero, Jesús
Paz Carrera, Jose Luis de
Fecha: 2017-06-17
Publicado en: International Journal of Molecular Sciences, 18 (6), 1-16.
Tipo de documento: Artículo
Resumen: FGF-1 is a potent mitogen that, by interacting simultaneously with Heparan Sulfate Glycosaminoglycan HSGAG and the extracellular domains of its membrane receptor (FGFR), generates an intracellular signal that finally leads to cell division. The overall structure of the ternary complex Heparin:FGF-1:FGFR has been finally elucidated after some controversy and the interactions within the ternary complex have been deeply described. However, since the structure of the ternary complex was described, not much attention has been given to the molecular basis of the interaction between FGF-1 and the HSGAG. It is known that within the complex, the carbohydrate maintains the same helical structure of free heparin that leads to sulfate groups directed towards opposite directions along the molecular axis. The precise role of single individual interactions remains unclear, as sliding and/or rotating of the saccharide along the binding pocket are possibilities difficult to discard. The HSGAG binding ...
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Cita: García Jiménez, M., Gil Caballero, S., Nieto Mesa, P.M., Canales, Á., Jiménez Barbero, J. y Paz Carrera, J.L.d. (2017). Interactions between a Heparin Trisaccharide Library and FGF-1 Analyzed by NMR Methods. International Journal of Molecular Sciences, 18 (6), 1-16.
Tamaño: 2.503Mb
Formato: PDF

URI: http://hdl.handle.net/11441/63977

DOI: 10.3390/ijms18061293

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