The principal neutralizing determinant of HIV‐1 located in V3 of gp120 forms a 12‐residue loop by internal hydrophobic interactions

FEBS Letters

Anglister, Jacob²  Kustanovich, Irina²  Hayek, Yehezkiel²  Matsushita, Shuzo¹  Zvi, Anat² 

[1] The Second Department of Internal Medicine, Kumamoto University Medical School, Honjo 1-1-1, Kumamoto 860, Japan;Department of Structural Biology, The Weizmann Institute of Science, Rehovot 76100, Israel

关键词: NMR;    1H;    Antibody;    Antigen conformation;    HIV-1;    gp120;   

DOI  :  10.1016/0014-5793(95)00669-Z

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The interactions of the peptide RP135a (RKSIRIQRGPGRAFVT), corresponding to residues 311–326 of gp120 of HIV-1_IIIB, with the anti-gp120 HIV-1_IIIB neutralizing antibody 0.5β were studied by NMR. The NOESY difference spectra measured using specifically deuterated derivatives of the peptide show exclusively the interactions of the deuterated residues both within the bound peptide and with the Fab fragment of the antibody. These measurements reveal hydrophobic interactions within the bound peptide between Ile-4, Ile-6 and Val-15 that create a 12-residue loop with these residues at the base and the conserved GPGR sequence at its top.

【 授权许可】

Unknown