The identification of a conserved binding motif within human papillomavirus type 16 E6 binding peptides, E6AP and E6BP

被引:64
作者
Elston, RC
Napthine, S
Doorbar, J
机构
[1] Natl Inst Med Res, Div Virol, London NW7 1AA, England
[2] Univ Cambridge, Dept Pathol, Div Virol, Cambridge CB2 1QP, England
关键词
D O I
10.1099/0022-1317-79-2-371
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
A 16-mer peptide library was screened using the yeast two-hybrid system to identify peptides which specifically interact with the human papillomavirus type 16 (HPV-16) E6 protein. Four different peptides were identified, three of which contained an EL-L/V-G motif. A fifth E6 binding peptide, derived from the putative tumour suppressor protein tuberin, was identified during a two-hybrid screen of a HeLa cDNA expression library. This peptide contained a D-I-L-G motif. Homology to the peptides was found within the E6 binding proteins E6AP and EG-BP. A synthetic peptide containing the ELLG motif blocked the interaction of E6 with both EG-AP and E6-BP. The data suggest that E6 interacts through a structurally similar binding domain present within a number of cellular proteins.
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页码:371 / 374
页数:4
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