3RBB
HIV-1 NEF protein in complex with engineered HCK SH3 domain
Summary for 3RBB
| Entry DOI | 10.2210/pdb3rbb/pdb |
| Related | 1AVZ 1EFN 2NEF 3REA 3REB |
| Descriptor | Protein Nef, Tyrosine-protein kinase HCK, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | hiv-1 nef, dileucine motif, sh3 domain, receptor internalization, pxxp motif, protein binding, viral protein |
| Biological source | HIV-1 M:B_ARV2/SF2 (HIV-1) More |
| Cellular location | Host cell membrane; Lipid-anchor; Cytoplasmic side (By similarity): P03407 Isoform p59-HCK: Membrane; Lipid-anchor. Isoform p60-HCK: Membrane; Lipid-anchor: P08631 |
| Total number of polymer chains | 4 |
| Total formula weight | 52699.03 |
| Authors | Horenkamp, F.A.,Schulte, A.,Weyand, M.,Geyer, M. (deposition date: 2011-03-29, release date: 2011-04-27, Last modification date: 2023-09-13) |
| Primary citation | Horenkamp, F.A.,Breuer, S.,Schulte, A.,Lulf, S.,Weyand, M.,Saksela, K.,Geyer, M. Conformation of the Dileucine-Based Sorting Motif in HIV-1 Nef Revealed by Intermolecular Domain Assembly. Traffic, 12:867-877, 2011 Cited by PubMed Abstract: The human immunodeficiency virus 1 (HIV-1) Nef protein is a pathogenicity factor required for effective progression to AIDS, which modulates host cell signaling pathways and T-cell receptor internalization. We have determined the crystal structure of Nef, allele SF2, in complex with an engineered SH3 domain of human Hck showing unnaturally tight binding and inhibitory potential toward Nef. This complex provides the most complete Nef structure described today, and explains the structural basis of the high affinity of this interaction. Intriguingly, the 33-residue C-terminal flexible loop is resolved in the structure by its interactions with a highly conserved hydrophobic groove on the core domain of an adjacent Nef molecule. The loop mediates the interaction of Nef with the cellular adaptor protein machinery for the stimulated internalization of surface receptors. The endocytic dileucine-based sorting motif is exposed at the tip of the acidic loop, giving the myristoylated Nef protein a distinctly dipolar character. The intermolecular domain assembly of Nef provides insights into a possible regulation mechanism for cargo trafficking. PubMed: 21477083DOI: 10.1111/j.1600-0854.2011.01205.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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