Molecular analysis of the interaction between HPV type 16 E6 and human E6-associated protein.
The complex formed between the human papillomavirus type 16 E6 protein and human E6-associated protein, which combine to ubiquitylate and degrade p53, has been studied by chemical crosslinking. Analysis of the interactions of proteins purified from Escherichia coli as well as proteins expressed in insect cells indicates that, while E6 has the capacity to form dimers, E6 and E6-associated protein interact as two monomers to form a heterologous dimer.
Daniels
P R
PR
YCRC Cancer Research Unit, University of York, UK.
Sanders
C M
CM
Coulson
P
P
Maitland
N J
NJ
D019281:Dimerization; D006801:Humans; D008025:Ligases / Q000235:genetics / Q000378:metabolism*; D009856:Oncogene Proteins, Viral / Q000235:genetics / Q000378:metabolism*; D027383:Papillomaviridae / Q000378:metabolism*; D011485:Protein Binding; D011994:Recombinant Proteins / Q000378:metabolism; D012097:Repressor Proteins; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism; D044767:Ubiquitin-Protein Ligases
C068651:E6 protein, Human papillomavirus type 16; D009856:Oncogene Proteins, Viral; D011994:Recombinant Proteins; D012097:Repressor Proteins; D016159:Tumor Suppressor Protein p53; C471639:UBE3A protein, human; D044767:Ubiquitin-Protein Ligases; D008025:Ligases