Electronic Resource
Near-physiological-temperature serial crystallography reveals conformations of SARS-CoV-2 main protease active site for improved drug repurposing
| العنوان: | Near-physiological-temperature serial crystallography reveals conformations of SARS-CoV-2 main protease active site for improved drug repurposing |
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| المؤلفون: | Department of Molecular Biology and Genetics; Department of Chemical and Biological Engineering; Department of Materials Science and Engineering, Demirci, Hasan (ORCID 0000-0002-9135-5397 & YÖK ID 307350); Dağ, Çağdaş; Yığın, Merve; Büyükdağ, Cengizhan; Ertem, Fatma Betül; Yıldırım, Günseli; Destan, Ebru; Güven, Ömür; Ayan, Esra; Yüksel, Büşra; Pekşen, Ayşe Buket; Göçenler, Oktay; Yücel, Ali Doğa; Can, Özgür; Ozabrahamyan, Serena; Shafiei, Alaleh; Akşit, Fulya; Tanısalı, Gökhan; Besler, Sabri Özkan, Durdağı, Serdar; Doğan, Berna; Avşar, Timuçin; Erol, İsmail; Çalış, Şeyma; Orhan, Müge D.; Aksoydan, Busecan; Şahin, Kader; Oktay, Lalehan; Tolu, İlayda; Olkan, Alpsu; Erdemoğlu, Ece; Yefanov, Oleksandr M.; Dao, E. Han; Hayes, Brandon; Liang, Mengning; Seaberg, Matthew H.; Hunter, Mark S.; Batyuk, Alex; Mariani, Valerio; Su, Zhen; Poitevin, Frederic; Yoon, Chun Hong; Kupitz, Christopher; Sierra, Raymond G.; Snell, Edward H. |
| المصدر: | Structure |
| بيانات النشر: | Elsevier 2021 |
| نوع الوثيقة: | Electronic Resource |
| Supplemental Data: | College of Sciences; Graduate School of Sciences and Engineering; School of Nursing |
| مستخلص: | The COVID-19 pandemic has resulted in 198 million reported infections and more than 4 million deaths as of July 2021 (covid19.who.int). Research to identify effective therapies for COVID-19 includes: (1) designing a vaccine as future protection; (2) de novo drug discovery; and (3) identifying existing drugs to repurpose them as effective and immediate treatments. To assist in drug repurposing and design, we determine two apo structures of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) main protease at ambient temperature by serial femtosecond X-ray crystallography. We employ detailed molecular simulations of selected known main protease inhibitors with the structures and compare binding modes and energies. The combined structural and molecular modeling studies not only reveal the dynamics of small molecules targeting the main protease but also provide invaluable opportunities for drug repurposing and structure-based drug design strategies against SARS-CoV-2. |
| مصطلحات الفهرس: | Biochemistry and molecular biology; Biophysics; Cell biology, Ambient temperature; Drug repurposing; Main protease; SARS-CoV-2; SFX, Journal article, pdf |
| URL: | Koç University Institutional Repository References TÜBİTAK |
| الاتاحة: | Open access content. Open access content |
| ملاحظة: | text/academic publication NSF-1231306; 118C270; BAU2020-0101 English |
| Other Numbers: | T9K oai:libdigitalcollections.ku.edu.tr:IR/9794 https://dx.doi.org/10.1016/j.str.2021.07.007 IR03134 1311243619 |
| المصدر المساهم: | KOC UNIV LIBR From OAIster®, provided by the OCLC Cooperative. |
| رقم الانضمام: | edsoai.on1311243619 |
| قاعدة البيانات: | OAIster |
| الوصف غير متاح. |