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Molecular architecture of native HIV-1 gp120 trimers

Author

Listed:
  • Jun Liu

    (Laboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, Maryland 20892, USA)

  • Alberto Bartesaghi

    (Laboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, Maryland 20892, USA)

  • Mario J. Borgnia

    (Laboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, Maryland 20892, USA)

  • Guillermo Sapiro

    (University of Minnesota, Minneapolis, Minnesota 55455, USA)

  • Sriram Subramaniam

    (Laboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, Maryland 20892, USA)

Abstract

HIV/AIDS: gp120 structure changes This paper investigates the structure of the HIV the gp120 coat protein of HIV by cryo-electron tomography and molecular modelling. Comparison of gp120 structures in an unbound state, bound to a neutralizing antibody and bound to CD4 cell surface protein provides insight into the conformational changes that occur during antibody neutralization and attachment to target cells.

Suggested Citation

  • Jun Liu & Alberto Bartesaghi & Mario J. Borgnia & Guillermo Sapiro & Sriram Subramaniam, 2008. "Molecular architecture of native HIV-1 gp120 trimers," Nature, Nature, vol. 455(7209), pages 109-113, September.
    • Handle: RePEc:nat:nature:v:455:y:2008:i:7209:d:10.1038_nature07159
    DOI: 10.1038/nature07159
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    Cited by:

    1. Lei Zhang & Gang Ren, 2012. "IPET and FETR: Experimental Approach for Studying Molecular Structure Dynamics by Cryo-Electron Tomography of a Single-Molecule Structure," PLOS ONE, Public Library of Science, vol. 7(1), pages 1-19, January.
    2. Terrence M Dobrowsky & Brian R Daniels & Robert F Siliciano & Sean X Sun & Denis Wirtz, 2010. "Organization of Cellular Receptors into a Nanoscale Junction during HIV-1 Adhesion," PLOS Computational Biology, Public Library of Science, vol. 6(7), pages 1-14, July.
    3. Javier Guenaga & Richard T Wyatt, 2012. "Structure-guided Alterations of the gp41-directed HIV-1 Broadly Neutralizing Antibody 2F5 Reveal New Properties Regarding its Neutralizing Function," PLOS Pathogens, Public Library of Science, vol. 8(7), pages 1-15, July.
    4. Durgadevi Parthasarathy & Karunakar Reddy Pothula & Sneha Ratnapriya & Héctor Cervera Benet & Ruth Parsons & Xiao Huang & Salam Sammour & Katarzyna Janowska & Miranda Harris & Joseph Sodroski & Priyam, 2024. "Conformational flexibility of HIV-1 envelope glycoproteins modulates transmitted/founder sensitivity to broadly neutralizing antibodies," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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