دورية أكاديمية
New insights into the molecular basis of lectin-carbohydrate interactions: a calorimetric and structural study of the association of hevein to oligomers of N-acetylglucosamine.
| العنوان: | New insights into the molecular basis of lectin-carbohydrate interactions: a calorimetric and structural study of the association of hevein to oligomers of N-acetylglucosamine. |
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| المؤلفون: | García-Hernández E; Departmento de Química, Universidad Autónoma Metropolitana Iztapalapa, México., Zubillaga RA, Rojo-Domínguez A, Rodríguez-Romero A, Hernández-Arana A |
| المصدر: | Proteins [Proteins] 1997 Dec; Vol. 29 (4), pp. 467-77. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Wiley-Liss Country of Publication: United States NLM ID: 8700181 Publication Model: Print Cited Medium: Print ISSN: 0887-3585 (Print) Linking ISSN: 08873585 NLM ISO Abbreviation: Proteins Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: New York, NY : Wiley-Liss Original Publication: New York : Alan R. Liss, c1986- |
| مواضيع طبية MeSH: | Antimicrobial Cationic Peptides* , Plant Lectins*, Acetylglucosamine/*chemistry , Carbohydrates/*chemistry , Lectins/*chemistry , Plant Proteins/*chemistry, Acetylglucosamine/metabolism ; Calorimetry ; Carbohydrate Metabolism ; Disaccharides/metabolism ; Hot Temperature ; Latex/chemistry ; Lectins/metabolism ; Magnetic Resonance Spectroscopy ; Plant Proteins/metabolism ; Polymers/chemistry ; Protein Binding ; Solvents ; Thermodynamics ; Trisaccharides/metabolism |
| مستخلص: | Isothermal titration calorimetry was used to characterize thermodynamically the association of hevein, a lectin from the rubber tree latex, with the dimer and trimer of N-acetylglucosamine (GlcNAc). Considering the changes in polar and apolar accessible surface areas due to complex formation, we found that the experimental binding heat capacities can be reproduced adequately by means of parameters used in protein-unfolding studies. The same conclusion applies to the association of the lectin concanavalin A with methyl-alpha-mannopyranoside. When reduced by the polar area change, binding enthalpy values show a minimal dispersion around 100 degrees C. These findings resemble the convergence observed in protein-folding events; however, the average of reduced enthalpies for lectin-carbohydrate associations is largely higher than that for the folding of proteins. Analysis of hydrogen bonds present at lectin-carbohydrate interfaces revealed geometries closer to ideal values than those observed in protein structures. Thus, the formation of more energetic hydrogen bonds might well explain the high association enthalpies of lectin-carbohydrate systems. We also have calculated the energy associated with the desolvation of the contact zones in the binding molecules and from it the binding enthalpy in vacuum. This latter resulted 20% larger than the interaction energy derived from the use of potential energy functions. |
| المشرفين على المادة: | 0 (Antimicrobial Cationic Peptides) 0 (Carbohydrates) 0 (Disaccharides) 0 (Latex) 0 (Lectins) 0 (Plant Lectins) 0 (Plant Proteins) 0 (Polymers) 0 (Solvents) 0 (Trisaccharides) 137295-60-4 (hevein) 41708-93-4 (chitotriose) 577-76-4 (chitobiose) V956696549 (Acetylglucosamine) |
| تواريخ الأحداث: | Date Created: 19971231 Date Completed: 19980210 Latest Revision: 20191102 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1002/(sici)1097-0134(199712)29:4<467::aid-prot7>3.0.co;2-5 |
| PMID: | 9408944 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 0887-3585 |
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| DOI: | 10.1002/(sici)1097-0134(199712)29:4<467::aid-prot7>3.0.co;2-5 |