کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1937472 1050717 2007 4 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Influenza viral hemagglutinin complicated shape is advantageous to its binding affinity for sialosaccharide receptor
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Influenza viral hemagglutinin complicated shape is advantageous to its binding affinity for sialosaccharide receptor
چکیده انگلیسی

Do the complexity and the bulkiness of a protein affect the affinity between protein and ligand? We attempted to investigate this problem by using ab initio fragment molecular orbital (FMO) method to calculate the binding energy between human influenza viral hemagglutinin (HA) and human oligo-saccharide receptor. We compared the binding energies of 4 different sizes of human A virus HA H3 subtype complexed with human receptor Neu5Ac(α2-6)Gal as a model. The full shape receptor binding domain complexed with Neu5Ac(α2-6)Gal had the highest binding energy 170.3 kcal/mol at the FMO-HF/STO-3G level, which was 52.3 kcal/mol higher than that of the smallest domain-receptor complex. These data provide the consideration of the backyard bulkiness beyond the binding site of protein to the protein-ligand stability.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 355, Issue 1, 30 March 2007, Pages 6–9
نویسندگان
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