کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5914848 | 1162759 | 2011 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Rapid identification of protein-protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR measurements
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کلمات کلیدی
HSQCCAPRIResidual dipolar coupling - اتصال دو قطبی باقی ماندهTev - به توTROSY - ترافیکNMR - تشدید مغناطیسی هستهای Protein–protein interaction - تعامل پروتئین-پروتئینRdc - طبقه همکفtransverse relaxation-optimized spectroscopy - طیف سنجی بهینه سازی اسپکترومتر عرضیHeteronuclear Single Quantum Correlation - همبستگی کوانتومی تک هسته ای تنهاTobacco etch virus - ویروس تنباکو اچProtein–protein docking - پیوند پروتئین پروتئینUbiquitin - یوبیکویتین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Protein-protein interactions are necessary for various cellular processes, and therefore, information related to protein-protein interactions and structural information of complexes is invaluable. To identify protein-protein interfaces using NMR, resonance assignments are generally necessary to analyze the data; however, they are time consuming to collect, especially for large proteins. In this paper, we present a rapid, effective, and unbiased approach for the identification of a protein-protein interface without resonance assignments. This approach requires only a single set of 2D titration experiments of a single protein sample, labeled with a unique combination of an 15N-labeled amino acid and several amino acids 13C-labeled on specific atoms. To rapidly obtain high resolution data, we applied a new pulse sequence for time-shared NMR measurements that allowed simultaneous detection of a Ï1-TROSY-type backbone 1H-15N and aromatic 1H-13C shift correlations together with single quantum methyl 1H-13C shift correlations. We developed a structure-based computational approach, that uses our experimental data to search the protein surfaces in an unbiased manner to identify the residues involved in the protein-protein interface. Finally, we demonstrated that the obtained information of the molecular interface could be directly leveraged to support protein-protein docking studies. Such rapid construction of a complex model provides valuable information and enables more efficient biochemical characterization of a protein-protein complex, for instance, as the first step in structure-guided drug development.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Structural Biology - Volume 174, Issue 3, June 2011, Pages 434-442
Journal: Journal of Structural Biology - Volume 174, Issue 3, June 2011, Pages 434-442
نویسندگان
Yuya Kodama, Michael L. Reese, Nobuhisa Shimba, Katsuki Ono, Eiji Kanamori, Volker Dötsch, Shuji Noguchi, Yoshifumi Fukunishi, Ei-ichiro Suzuki, Ichio Shimada, Hideo Takahashi,