THE PRINCIPAL NEUTRALIZING DETERMINANT OF HIV-1 LOCATED IN V3 OF GP120 FORMS A 12-RESIDUE LOOP BY INTERNAL HYDROPHOBIC INTERACTIONS

被引：19

作者：

ZVI, A

KUSTANOVICH, I

HAYEK, Y

MATSUSHITA, S

ANGLISTER, J

机构：

[1] WEIZMANN INST SCI,DEPT BIOL STRUCT,IL-76100 REHOVOT,ISRAEL

[2] KUMAMOTO UNIV,SCH MED,DEPT INTERNAL MED 2,KUMAMOTO 860,JAPAN

来源：

FEBS LETTERS | 1995年 / 368卷 / 02期

基金：

以色列科学基金会;

关键词：

NMR; H-1; ANTIBODY; ANTIGEN CONFORMATION; HIV-1; GP120;

D O I：

10.1016/0014-5793(95)00669-Z

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 0.5 beta 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.

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页码：267 / 270

页数：4

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