2MA9
HIV-1 Vif SOCS-box and Elongin BC solution structure
Summary for 2MA9
Entry DOI | 10.2210/pdb2ma9/pdb |
Related | 3DCG |
NMR Information | BMRB: 19333 |
Descriptor | Virion infectivity factor, Transcription elongation factor B polypeptide 2, Transcription elongation factor B polypeptide 1 (3 entities in total) |
Functional Keywords | hiv-1 vif socs-box, elongin bc, viral protein-protein binding complex, viral protein/protein binding |
Biological source | Human immunodeficiency virus type 1 (HIV-1) More |
Cellular location | Host cytoplasm: P12504 Nucleus : Q15370 Q15369 |
Total number of polymer chains | 3 |
Total formula weight | 27483.37 |
Authors | Lu, Z.,Bergeron, J.R.,Atkinson, R.A.,Schaller, T.,Veselkov, D.A.,Oregioni, A.,Yang, Y.,Matthews, S.J.,Malim, M.H.,Sanderson, M.R. (deposition date: 2013-07-01, release date: 2013-12-11, Last modification date: 2024-05-01) |
Primary citation | Lu, Z.,Bergeron, J.R.,Atkinson, R.A.,Schaller, T.,Veselkov, D.A.,Oregioni, A.,Yang, Y.,Matthews, S.J.,Malim, M.H.,Sanderson, M.R. Insight into the HIV-1 Vif SOCS-box-ElonginBC interaction. OPEN BIOLOGY, 3:130100-130100, 2013 Cited by PubMed Abstract: The HIV-1 viral infectivity factor (Vif) neutralizes cell-encoded antiviral APOBEC3 proteins by recruiting a cellular ElonginB (EloB)/ElonginC (EloC)/Cullin5-containing ubiquitin ligase complex, resulting in APOBEC3 ubiquitination and proteolysis. The suppressors-of-cytokine-signalling-like domain (SOCS-box) of HIV-1 Vif is essential for E3 ligase engagement, and contains a BC box as well as an unusual proline-rich motif. Here, we report the NMR solution structure of the Vif SOCS-ElonginBC (EloBC) complex. In contrast to SOCS-boxes described in other proteins, the HIV-1 Vif SOCS-box contains only one α-helical domain followed by a β-sheet fold. The SOCS-box of Vif binds primarily to EloC by hydrophobic interactions. The functionally essential proline-rich motif mediates a direct but weak interaction with residues 101-104 of EloB, inducing a conformational change from an unstructured state to a structured state. The structure of the complex and biophysical studies provide detailed insight into the function of Vif's proline-rich motif and reveal novel dynamic information on the Vif-EloBC interaction. PubMed: 24225024DOI: 10.1098/rsob.130100 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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