6K6N

Crystal structure of SIVmac239 Nef protein

Summary for 6K6N

• Entry DOI: 10.2210/pdb6k6n/pdb
• Descriptor: Protein Nef (2 entities in total)
• Functional Keywords: siv, nef, accesory protein, viral protein
• Biological source: Simian immunodeficiency virus (SIV)
• Total number of polymer chains: 1
• Total formula weight: 20545.02

Authors

Hirao, K.,Andrews, S.,Kuroki, K.,Kusaka, H.,Tadokoro, T.,Kita, S.,Ose, T.,Rowland-Jones, S.,Maenaka, K. (deposition date: 2019-06-04, release date: 2020-03-25, Last modification date: 2023-11-22)

Primary citation

Hirao, K.,Andrews, S.,Kuroki, K.,Kusaka, H.,Tadokoro, T.,Kita, S.,Ose, T.,Rowland-Jones, S.L.,Maenaka, K.
Structure of HIV-2 Nef Reveals Features Distinct from HIV-1 Involved in Immune Regulation.
Iscience, 23:100758-100758, 2020

PubMed Abstract: The human immunodeficiency virus (HIV) accessory protein Nef plays a major role in establishing and maintaining infection, particularly through immune evasion. Many HIV-2-infected people experience long-term viral control and survival, resembling HIV-1 elite control. HIV-2 Nef has overlapping but also distinct functions from HIV-1 Nef. Here we report the crystal structure of HIV-2 Nef core. The di-leucine sorting motif forms a helix bound to neighboring molecules, and moreover, isothermal titration calorimetry demonstrated that the CD3 endocytosis motif can directly bind to HIV-2 Nef, ensuring AP-2-mediated endocytosis for CD3. The highly conserved C-terminal region forms a α-helix, absent from HIV-1. We further determined the structure of simian immunodeficiency virus (SIV) Nef harboring this region, demonstrating similar C-terminal α-helix, which may contribute to AP-1 binding for MHC-I downregulation. These results provide insights into the distinct pathogenesis of HIV-2 infection.

PubMed: 31927483
DOI: 10.1016/j.isci.2019.100758

Experimental method

X-RAY DIFFRACTION (2.0002 Å)