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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Detalles Bibliográficos

Publicado en:	EMBO J
Principais autores:	Denhez, F, Heimann, B, d'Auriol, L, Graf, T, Coquillaud, M, Coll, J, Galibert, F, Moelling, K, Stehelin, D, Ghysdael, J
Formato:	Artigo
Idioma:	Inglês
Publicado:	Nature Publishing Group 1988
Assuntos:	Research Article
Acceso en liña:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC454352/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2835233/ https://ncbi.nlm.nih.govhttps://doi.org/10.1002/j.1460-2075.1988.tb02843.x
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