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 bg chemical crosslinking. Analysis of the interactions of proteins purified from Escherichia coli as wen 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. (C) 1997 Federation of European Biochemical Societies.
|Number of pages||5|
|Publication status||Published - 13 Oct 1997|
- human papillomavirus
- E6-associated protein
- HUMAN PAPILLOMAVIRUS TYPE-16