التفاصيل البيبلوغرافية
| العنوان: |
Characterization of possible binding of loxapine to the HAV 2C hexamer. |
| المؤلفون: |
Mami Matsuda, Asuka Hirai-Yuki, Osamu Kotani, Michiyo Kataoka, Xin Zheng, Daisuke Yamane, Masaru Yokoyama, Koji Ishii, Masamichi Muramatsu, Ryosuke Suzuki |
| سنة النشر: |
2024 |
| المجموعة: |
Smithsonian Institution: Figshare |
| مصطلحات موضوعية: |
Biochemistry, Medicine, Cell Biology, Molecular Biology, Pharmacology, Cancer, Mental Health, Infectious Diseases, Virology, Biological Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, viruses containing mutations, viral rna replication, resistant mutations impede, provide novel insights, molecular dynamics simulations, inhibit viral entry, exhibited strong inhibition, div >< p, >< sup ><, loxapine inhibits replication, intrahepatic hav rna, fecal hav rna, antiviral drugs currently, loxapine succinate resulted, hav protein 2c, loxapine succinate, >, loxapine suggested, loxapine binds |
| الوصف: |
(A) Root-mean-square deivations (RMSDs) between the initial model structure and the structures at the indicated time points during the molecular dynamics (MD) simulation of the 2C hexamer. (B) 2C hexamer structure at 200 ns of MD simulations. Red sticks show the side chains of the F1089 and C1111 amino acid residues. Orange, light green, and light blue portions indicate the pocket-binding domain [ 6 ], ATPase active sites [ 6 ] and membrane-binding motif [ 16 ], respectively. (C) Enlarged view of the region including the F1089 and C1111 amino acid residues. (D) Molecular patches relevant to hydrophobic and electrostatic interactions. Green portions indicate the hydrophobic patches that potentially are involved in the interactions between the hydrophobic moieties of molecules. Blue portions indicate the positively charged patches that potentially interact with negatively charged molecules. (E) Distribution of binding energies of the top-100 binding poses of the structure of the 2C-loxapine complex. Line indicates mean value. (F) RMSDs during the MD simulation of the 2C-loxapine complex. (G) Binding modes between 2C and loxapine. The two mutation sites (F1089 and C1111) are shown as red sticks. The red dotted lines show the arene interactions between loxapine and F1089. Blue, red, and green portions in the loxapine structure indicate nitrogen, oxygen, and chlorine atoms, respectively. The green and blue patches show the hydrophobic and positively charged regions, respectively. (H) Effects on the binding affinity of loxapine for the 2C hexamer. Changes in the binding affinity of loxapine were calculated using the structure of the 2C-loxapine complex obtained at 200 ns of MD simulations using the Protein Design application of MOE. Statistical significance was determined using a two-tailed non-paired Student’s t test. ** P <0.01 (vs. wild type (WT)). |
| نوع الوثيقة: |
still image |
| اللغة: |
unknown |
| Relation: |
https://figshare.com/articles/figure/Characterization_of_possible_binding_of_loxapine_to_the_HAV_2C_hexamer_/25403278 |
| DOI: |
10.1371/journal.ppat.1012091.g004 |
| الاتاحة: |
https://doi.org/10.1371/journal.ppat.1012091.g004 |
| Rights: |
CC BY 4.0 |
| رقم الانضمام: |
edsbas.9177991C |
| قاعدة البيانات: |
BASE |