Characterization of the galectin-1 carbohydrate recognition domain in terms of solvent occupancy
Human galectin-1, a galactosil-terminal sugar binding soluble protein, is a potent multifunctional effector that participates in specific protein-carbohydrate and protein-protein interactions. Recent studies revealed that it plays a key role as a modulator of cellular differentiation and immunologic...
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2007
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paper:paper_15206106_v111_n25_p7360_Lella2023-06-08T16:18:57Z Characterization of the galectin-1 carbohydrate recognition domain in terms of solvent occupancy Martí, Marcelo Adrián Estrin, Dario Ariel Carbohydrates Computer simulation Distribution functions Free energy Immunology Molecular dynamics Carbohydrate recognition domain Protein-carbohydrate Protein-protein interactions Proteins Human galectin-1, a galactosil-terminal sugar binding soluble protein, is a potent multifunctional effector that participates in specific protein-carbohydrate and protein-protein interactions. Recent studies revealed that 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 of molecular dynamics simulations. Water sites (ws) were identified in terms of radial and angular distribution functions, and properties such as water residence times, interaction energies, and free-energy contributions were evaluated for those sites. Our results allowed us to correlate the thermodynamic properties of the ws and their binding pattern with the N-acetilgalactoside ligand. These results let us further infer that the water molecules located at the ws, which exhibit much more favorable binding, are the ones replaced by -OH groups of the sugar. © 2007 American Chemical Society. Fil:Martí, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Estrin, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2007 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15206106_v111_n25_p7360_Lella http://hdl.handle.net/20.500.12110/paper_15206106_v111_n25_p7360_Lella |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Carbohydrates Computer simulation Distribution functions Free energy Immunology Molecular dynamics Carbohydrate recognition domain Protein-carbohydrate Protein-protein interactions Proteins |
| spellingShingle |
Carbohydrates Computer simulation Distribution functions Free energy Immunology Molecular dynamics Carbohydrate recognition domain Protein-carbohydrate Protein-protein interactions Proteins Martí, Marcelo Adrián Estrin, Dario Ariel Characterization of the galectin-1 carbohydrate recognition domain in terms of solvent occupancy |
| topic_facet |
Carbohydrates Computer simulation Distribution functions Free energy Immunology Molecular dynamics Carbohydrate recognition domain Protein-carbohydrate Protein-protein interactions Proteins |
| description |
Human galectin-1, a galactosil-terminal sugar binding soluble protein, is a potent multifunctional effector that participates in specific protein-carbohydrate and protein-protein interactions. Recent studies revealed that 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 of molecular dynamics simulations. Water sites (ws) were identified in terms of radial and angular distribution functions, and properties such as water residence times, interaction energies, and free-energy contributions were evaluated for those sites. Our results allowed us to correlate the thermodynamic properties of the ws and their binding pattern with the N-acetilgalactoside ligand. These results let us further infer that the water molecules located at the ws, which exhibit much more favorable binding, are the ones replaced by -OH groups of the sugar. © 2007 American Chemical Society. |
| author |
Martí, Marcelo Adrián Estrin, Dario Ariel |
| author_facet |
Martí, Marcelo Adrián Estrin, Dario Ariel |
| author_sort |
Martí, Marcelo Adrián |
| title |
Characterization of the galectin-1 carbohydrate recognition domain in terms of solvent occupancy |
| title_short |
Characterization of the galectin-1 carbohydrate recognition domain in terms of solvent occupancy |
| title_full |
Characterization of the galectin-1 carbohydrate recognition domain in terms of solvent occupancy |
| title_fullStr |
Characterization of the galectin-1 carbohydrate recognition domain in terms of solvent occupancy |
| title_full_unstemmed |
Characterization of the galectin-1 carbohydrate recognition domain in terms of solvent occupancy |
| title_sort |
characterization of the galectin-1 carbohydrate recognition domain in terms of solvent occupancy |
| publishDate |
2007 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15206106_v111_n25_p7360_Lella http://hdl.handle.net/20.500.12110/paper_15206106_v111_n25_p7360_Lella |
| work_keys_str_mv |
AT martimarceloadrian characterizationofthegalectin1carbohydraterecognitiondomainintermsofsolventoccupancy AT estrindarioariel characterizationofthegalectin1carbohydraterecognitiondomainintermsofsolventoccupancy |
| _version_ |
1768546507370266624 |