کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5371715 1503965 2009 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Molecular modeling, dynamics and docking studies of Purine Nucleoside Phosphorylase from Streptococcus pyogenes
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی تئوریک و عملی
پیش نمایش صفحه اول مقاله
Molecular modeling, dynamics and docking studies of Purine Nucleoside Phosphorylase from Streptococcus pyogenes
چکیده انگلیسی

Purine Nucleoside Phosphorylase (PNP) catalyzes the reversible phosphorolysis of N-glycosidic bonds of purine nucleosides and deoxynucleosides, except for adenosine, to generate ribose 1-phosphate and the purine base. PNP has been submitted to intensive structural studies. This work describes for the first time a structural model of PNP from Streptococcus pyogenes (SpPNP). We modeled the complexes of SpPNP with six different ligands in order to determine the structural basis for specificity of these ligands against SpPNP. Molecular dynamics (MD) simulations were performed in order to evaluate the overall stability of SpPNP model. The analysis of the MD simulation was assessed mainly by principal component analysis (PCA) to explore the trimeric structure behavior. Structural comparison, between SpPNP and human PNP, was able to identify the main features responsible for differences in ligand-binding affinities, such as mutation in the purine-binding site and in the second phosphate-binding site. The PCA analysis suggests a different behavior for each subunit in the trimer structure.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biophysical Chemistry - Volume 142, Issues 1–3, June 2009, Pages 7-16
نویسندگان
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