1NJ0
NMR structure of a V3 (MN isolate) peptide bound to 447-52D, a human HIV-1 neutralizing antibody
Summary for 1NJ0
| Entry DOI | 10.2210/pdb1nj0/pdb |
| Related | 1NIZ |
| Descriptor | Exterior membrane glycoprotein(GP120) (1 entity in total) |
| Functional Keywords | peptide-antibody complex, b-hairpin, viral protein |
| Biological source | Human immunodeficiency virus 1 |
| Cellular location | Transmembrane protein gp41: Virion membrane; Single-pass type I membrane protein. Surface protein gp120: Virion membrane; Peripheral membrane protein: P05877 |
| Total number of polymer chains | 1 |
| Total formula weight | 1907.27 |
| Authors | Sharon, M.,Kessler, N.,Levy, R.,Zolla-Pazner, S.,Gorlach, M.,Anglister, J. (deposition date: 2002-12-30, release date: 2003-02-25, Last modification date: 2024-05-22) |
| Primary citation | Sharon, M.,Kessler, N.,Levy, R.,Zolla-Pazner, S.,Gorlach, M.,Anglister, J. Alternative Conformations of HIV-1 V3 Loops Mimic beta Hairpins in Chemokines, Suggesting a Mechanism for Coreceptor Selectivity. Structure, 11:225-236, 2003 Cited by PubMed Abstract: The V3 loop of the HIV-1 envelope glycoprotein gp120 is involved in binding to the CCR5 and CXCR4 coreceptors. The structure of an HIV-1(MN) V3 peptide bound to the Fv of the broadly neutralizing human monoclonal antibody 447-52D was solved by NMR and found to be a beta hairpin. This structure of V3(MN) was found to have conformation and sequence similarities to beta hairpins in CD8 and CCR5 ligands MIP-1alpha, MIP-1beta, and RANTES and differed from the beta hairpin of a V3(IIIB) peptide bound to the strain-specific murine anti-gp120(IIIB) antibody 0.5beta. In contrast to the structure of the bound V3(MN) peptide, the V3(IIIB) peptide resembles a beta hairpin in SDF-1, a CXCR4 ligand. These data suggest that the 447-52D-bound V3(MN) and the 0.5beta-bound V3(IIIB) structures represent alternative V3 conformations responsible for selective interactions with CCR5 and CXCR4, respectively. PubMed: 12575942DOI: 10.1016/S0969-2126(03)00011-X PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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