دورية أكاديمية
أعرض في EDS

Cooperative Membrane Binding of HIV-1 Matrix Proteins.

التفاصيل البيبلوغرافية
العنوان: Cooperative Membrane Binding of HIV-1 Matrix Proteins.
المؤلفون: Banerjee P; Department of Chemistry, Chicago Center for Theoretical Chemistry, Institute for Biophysical Dynamics, and James Franck Institute, The University of Chicago, Chicago, Illinois 60637, United States., Monje-Galvan V; Department of Chemistry, Chicago Center for Theoretical Chemistry, Institute for Biophysical Dynamics, and James Franck Institute, The University of Chicago, Chicago, Illinois 60637, United States., Voth GA; Department of Chemistry, Chicago Center for Theoretical Chemistry, Institute for Biophysical Dynamics, and James Franck Institute, The University of Chicago, Chicago, Illinois 60637, United States.
المصدر: The journal of physical chemistry. B [J Phys Chem B] 2024 Mar 21; Vol. 128 (11), pp. 2595-2606. Date of Electronic Publication: 2024 Mar 13.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: American Chemical Society Country of Publication: United States NLM ID: 101157530 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-5207 (Electronic) Linking ISSN: 15205207 NLM ISO Abbreviation: J Phys Chem B Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, D.C. : American Chemical Society, c1997-
مواضيع طبية MeSH: gag Gene Products, Human Immunodeficiency Virus*/metabolism , HIV-1*/metabolism, Virus Assembly ; Cell Membrane/metabolism ; Protein Binding ; Viral Matrix Proteins/chemistry
مستخلص: The HIV-1 assembly process begins with a newly synthesized Gag polyprotein being targeted to the inner leaflet of the plasma membrane of the infected cells to form immature viral particles. Gag-membrane interactions are mediated through the myristoylated (Myr) N-terminal matrix (MA) domain of Gag, which eventually multimerize on the membrane to form trimers and higher order oligomers. The study of the structure and dynamics of peripheral membrane proteins like MA has been challenging for both experimental and computational studies due to the complex transient dynamics of protein-membrane interactions. Although the roles of anionic phospholipids (PIP2, PS) and the Myr group in the membrane targeting and stable membrane binding of MA are now well-established, the cooperative interactions between the MA monomers and MA-membrane remain elusive in the context of viral assembly and release. Our present study focuses on the membrane binding dynamics of a higher order oligomeric structure of MA protein (a dimer of trimers), which has not been explored before. Employing time-lagged independent component analysis (tICA) to our microsecond-long trajectories, we investigate conformational changes of the matrix protein induced by membrane binding. Interestingly, the Myr switch of an MA monomer correlates with the conformational switch of adjacent monomers in the same trimer. Together, our findings suggest complex protein dynamics during the formation of the immature HIV-1 lattice; while MA trimerization facilitates Myr insertion, MA trimer-trimer interactions in the immature lattice can hinder the same.
التعليقات: Update of: bioRxiv. 2023 Sep 24;:. (PMID: 37790356)
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معلومات مُعتمدة: R01 GM116961 United States GM NIGMS NIH HHS; S10 OD028655 United States OD NIH HHS; U54 AI170855 United States AI NIAID NIH HHS
المشرفين على المادة: 0 (gag Gene Products, Human Immunodeficiency Virus)
0 (Viral Matrix Proteins)
تواريخ الأحداث: Date Created: 20240313 Date Completed: 20240322 Latest Revision: 20240327
رمز التحديث: 20240327
مُعرف محوري في PubMed: PMC10962350
DOI: 10.1021/acs.jpcb.3c06222
PMID: 38477117
قاعدة البيانات: MEDLINE
الوصف
تدمد:1520-5207
DOI:10.1021/acs.jpcb.3c06222