Solution conformation of a peptide corresponding to residues 151-172 of HIV-1 integrase using NMR and CD spectroscopy

被引：0

作者：

Cheng, JW ^{[1
]}

Cheng, CC ^{[1
]}

Lyu, PC ^{[1
]}

Chen, ST ^{[1
]}

Lin, TH ^{[1
]}

机构：

[1] ACAD SINICA, INST BIOL CHEM, TAIPEI, TAIWAN

来源：

INTERNATIONAL JOURNAL OF PEPTIDE AND PROTEIN RESEARCH | 1996年 / 47卷 / 1-2期

关键词：

circular dichroism; dimerization; HIV-1; integrase; nuclear magnetic resonance; predicted leucine zipper motif; solution conformation;

D O I：

暂无

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 solution structure of a synthetic peptide corresponding to residues 151-172 of HIV-1 integrase has been determined by NMR and CD spectroscopy. Residues 151-172 of HIV-1 integrase were predicted to be an cc-helix and to be responsible for the oligomerization of HIV-1 integrase. Two-dimensional H-1 NMR and CD studies indicate that this synthetic peptide adopts an amphipathic alpha-helical conformation in TFE-containing solution. However, concentration-dependent CD studies reveal that this peptide motif does not form dimers or oligomers in solution as predicted. These results are in agreement with the crystal structure of the catalytic domain of HIV-1 integrase reported recently. (C) Munksgaard 1996.

引用

页码：117 / 122

页数：6

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