Replacement of lys 622 in the ATP binding domain of P100gag-mil abolishes the in vitro autophosphorylation of the protein and the biological properties of the v-mil oncogene of MH2 virus.

Lysine 622 in the ATP-binding domain of P100gag-mil, the translation product of the v-mil oncogene of MH2, has been replaced with methionine using oligonucleotide site-directed mutagenesis. This substitution results in the inactivation of the serine/threonine-specific autophosphorylation of P100gag-...

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Hlavní autoři: Denhez, F, Heimann, B, d'Auriol, L, Graf, T, Coquillaud, M, Coll, J, Galibert, F, Moelling, K, Stehelin, D, Ghysdael, J
Médium: Artigo
Jazyk:Inglês
Vydáno: 1988
Témata:
Research Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC454352/
https://ncbi.nlm.nih.gov/pubmed/2835233
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