1B03
SOLUTION STRUCTURE OF THE ANTIBODY-BOUND HIV-1IIIB V3 PEPTIDE
Summary for 1B03
| Entry DOI | 10.2210/pdb1b03/pdb |
| Descriptor | PROTEIN (P1053 PEPTIDE) (1 entity in total) |
| Functional Keywords | p1053 structure, viral protein |
| Cellular location | Virion membrane : Q79428 |
| Total number of polymer chains | 1 |
| Total formula weight | 2017.41 |
| Authors | Tugarinov, V.,Zvi, A.,Levy, R.,Anglister, J. (deposition date: 1998-11-17, release date: 1998-11-25, Last modification date: 2023-12-27) |
| Primary citation | Tugarinov, V.,Zvi, A.,Levy, R.,Anglister, J. A cis proline turn linking two beta-hairpin strands in the solution structure of an antibody-bound HIV-1IIIB V3 peptide. Nat.Struct.Biol., 6:331-335, 1999 Cited by PubMed Abstract: The refined solution structure of an 18-residue HIV-1IIIB V3 peptide in complex with the Fv fragment of an anti-gp120 antibody reveals an unexpected type VI beta-turn comprising residues RGPG at the center of a beta-hairpin. The central glycine and proline of this turn are linked by a cis peptide bond. The residues of the turn interact extensively with the antibody Fv. 15N[1H] NOE measurements show that the backbone of the peptide, including the central QRGPGR loop, is well ordered in the complex. The solution structure is significantly different from the X-ray structures of HIV-1MN V3 peptides bound to anti-peptide antibodies. These differences could be due to a two-residue (QR) insertion preceding the GPGR sequence in the HIV-1IIIB strain, and the much longer peptide epitope immobilized by the anti-gp120 antibody. PubMed: 10201400DOI: 10.1038/7567 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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