Structural basis of CD4 downregulation by HIV-1 Nef

• Published in: Nature structural & molecular biology Vol. 27; no. 9; pp. 822 - 828
• Main Authors: Kwon, Yonghwa, Kaake, Robyn M., Echeverria, Ignacia, Suarez, Marissa, Karimian Shamsabadi, Mohammad, Stoneham, Charlotte, Ramirez, Peter W., Kress, Jacob, Singh, Rajendra, Sali, Andrej, Krogan, Nevan, Guatelli, John, Jia, Xiaofei
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group US 01.09.2020; Nature Publishing Group
• Subjects: 101/58; 13/31; 631/326/596; 631/535/1266; 82; Adaptor Protein Complex 2 - chemistry; Adaptor Protein Complex 2 - metabolism; Adaptor proteins; Binding; Biochemistry; Biological Microscopy; Biomedical and Life Sciences; CD4 antigen; CD4 Antigens - chemistry; CD4 Antigens - metabolism; Cell surface; Cell surface receptors; Clathrin; Crystal structure; Crystallography; Crystallography, X-Ray; Down-regulation; Drug development; Endocytosis; Fusion protein; HeLa Cells; HIV; HIV Infections - metabolism; HIV-1 - physiology; Host-Pathogen Interactions; Human immunodeficiency virus; Humans; Immune clearance; Immunosurveillance; Life Sciences; Major histocompatibility complex; Membrane Biology; Models, Molecular; Mutagenesis; nef Gene Products, Human Immunodeficiency Virus - chemistry; nef Gene Products, Human Immunodeficiency Virus - metabolism; Nef protein; Pathogenesis; Protein Binding; Protein Conformation; Protein Domains; Protein Structure; Proteins; Viruses

The HIV-1 Nef protein suppresses multiple immune surveillance mechanisms to promote viral pathogenesis and is an attractive target for the development of novel therapeutics. A key function of Nef is to remove the CD4 receptor from the cell surface by hijacking clathrin- and adaptor protein complex 2...