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Molecular dynamic analyses of the interaction of SARS-CoV-1 or 2 variants with various angiotensin-converting enzyme-2 species.
Aloufi, Abeer S; El-Arabey, Amr Ahmed; Eltayb, Wafa Ali; Elsayim, Rasha; Marenga, Hanin S; Modafer, Yosra; Awadalla, Maaweya E; Mohapatra, Pranab K; Mohapatra, Ranjan K; Abdalla, Mohnad.
Afiliación
  • Aloufi AS; Department of Biology, College of Science, princess Nourah bint Abdulrahman University, Riyadh, Saudi Arabia.
  • El-Arabey AA; Department of Pharmacology and Toxicology, Faculty of Pharmacy, Al-Azhar University, Cairo, Egypt.
  • Eltayb WA; Biotechnology Department, Faculty of Science and Technology, Shendi University, Shendi, Nher Anile, Sudan.
  • Elsayim R; Department of Botany and Microbiology, College of Science, King Saud University, Riyadh, Saudi Arabia.
  • Marenga HS; Department of Pharmaceutical chemistry, College of pharmacy, King Saud University, Riyadh, Saudi Arabia.
  • Modafer Y; Department of Biology, Faculty of Science, Jazan university, Jazan, Saudi Arabia.
  • Awadalla ME; Research Center, King Fahad Medical City, Riyadh, Saudi Arabia.
  • Mohapatra PK; Department of Chemistry, C. V. Raman Global University, Bhubaneswar, Odisha, India.
  • Mohapatra RK; Department of Chemistry, Government College of Engineering, Keonjhar, Odisha, India.
  • Abdalla M; Pediatric Research Institute, Children's Hospital Affiliated to Shandong University, Jinan, China.
J Biomol Struct Dyn ; : 1-10, 2024 Feb 12.
Article en En | MEDLINE | ID: mdl-38344933
ABSTRACT
The transmembrane glycoprotein angiotensin-converting enzyme 2 (ACE2) is a key component of the renin-angiotensin system (RAS). It was shown to be the receptor of severe acute respiratory syndrome coronavirus 2 in the COVID-19 outbreak (SARS-COV-2). Furthermore, ACE2 aids in the transport of amino acids across the membrane. ACE2 is lost from the membrane, resulting in soluble ACE2 (sACE2). We aim to examine the structural conformation alterations between SARS-CoV-1 or 2 variants at various periods with ACE2 from various sources, particularly in the area where it interacts with the viral protein and the receptor. It is important to study the molecular dynamics of ACE2/SARS-COV RBD when the structure is available on the database. Here we analyzed the crystal structure of ACE2 from Human, Dog, Mus, Cat, and Bat ACE2 in complex with RBD from SARS-COV-1 and SARS-COV-2. The result shows, there is a variation in the type of residues, number of contact atoms and hydrogen bonds in ACE2 and RBD during the interaction interfaces. By using molecular dynamics simulation, we can measure RMSD, RMSF, SASA, Rg and the difference in the percentage of α helix and ß strand. As bat ACE2 & SARS-CoV-2 RBD found to have a high amount of ß strand compared to another structure complex, while hACE2 & SARS-CoV-1 RBD has fewer amounts of ß strand. Our study provides a deep view of the structure which is available and a summary of many works around ACE2/SARS-CoV RBD interaction.Communicated by Ramaswamy H. Sarma.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: J Biomol Struct Dyn Año: 2024 Tipo del documento: Article País de afiliación: Arabia Saudita Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: J Biomol Struct Dyn Año: 2024 Tipo del documento: Article País de afiliación: Arabia Saudita Pais de publicación: Reino Unido