Characterization of the Galectin-1 Carbohydrate Recognition Domain in Terms of Solvent Occupancy

详细信息    查看全文

• 作者：Santiago Di Lella ; Marcelo A. Mart&iacute ; R. Mar&iacute ; a S. Á ; lvarez ; Dar&iacute ; o A. Estrin ; Juan C. D&iacute ; az Ricci
• 刊名：Journal of Physical Chemistry B
• 出版年：2007
• 出版时间：June 28, 2007
• 年：2007
• 卷：111
• 期：25
• 页码：7360 - 7366
• 全文大小：270K
• 年卷期：v.111,no.25(June 28, 2007)
• ISSN：1520-5207

文摘

Human galectin-1, a galactosil-terminal sugar binding soluble protein, is a potent multifunctional effectorthat participates in specific protein-carbohydrate and protein-protein interactions. Recent studies revealedthat it plays a key role as a modulator of cellular differentiation and immunological response. In this work,we have investigated the solvation properties of the carbohydrate recognition domain of Gal-1 by means ofmolecular dynamics simulations. Water sites (ws) were identified in terms of radial and angular distributionfunctions, and properties such as water residence times, interaction energies, and free-energy contributionswere evaluated for those sites. Our results allowed us to correlate the thermodynamic properties of the wsand their binding pattern with the N-acetilgalactoside ligand. These results let us further infer that the watermolecules located at the ws, which exhibit much more favorable binding, are the ones replaced by -OHgroups of the sugar.