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A cis proline turn linking two β-hairpin strands in the solution structure of an antibody-bound HIV-1IIIB V3 peptide

Nature Structural Biology volume 6, pages 331–335 (1999)Cite this article

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 β-turn comprising residues RGPG at the center of a β-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.

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Figure 1: a, The amide fingerprint region of the 600 MHz [F1-13C/15N, F2-13C/15N]-filtered NOESY spectrum of the unlabeled P1053 in complex with the [U-13C/15N]-0.5β Fv.
Figure 2: a, The alpha region of the 500 MHz 13C-edited NOESY spectrum of P1053 doubly labeled at positions Gly 12, Pro 13 and Gly 14.
Figure 3: a, A stereo view of the best-fit backbone superposition of 35 structures of segment P1053 (residues Arg 4–Gly 21) bound to 0.5β Fv.
Figure 4: The steady state 15N{1H} NOE values, amide 15N T1, T2 relaxation times, and the calculated order parameters (S2) of the antibody-bound P1053 versus residue numbers.

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Acknowledgements

We thank F. Delaglio (NIH, Bethesda, USA) for NMR processing software, A. Bax (NIH, Bethesda, USA) and S. Grzesiek (Jülich Research Center, Germany) for pulse sequences and continuous assistance in the project. We are indebted to S. Matsushita (Kumamoto University, Japan) for the 0.5β hybridoma cells, and to A. Kapitkovsky and Y. Hayek (Weizmann Institute) for peptide synthesis and purification. G. Faiman and A. Horovitz (Weizmann Institute) are acknowledged for the joint effort to establish the Fv expression system. This research was supported by an NIH grant and the Minerva Foundation.

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  1. Department of Structural Biology, The Weizmann Institute of Science, Rehovot, 76100, Israel

    Vitali Tugarinov, Anat Zvi, Rina Levy & Jacob Anglister

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  1. Vitali Tugarinov
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Correspondence to Jacob Anglister.

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Tugarinov, V., Zvi, A., Levy, R. et al. A cis proline turn linking two β-hairpin strands in the solution structure of an antibody-bound HIV-1IIIB V3 peptide. Nat Struct Mol Biol 6, 331–335 (1999). https://doi.org/10.1038/7567

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