Interaction of the p85 subunit of PI 3-kinase and its N-terminal SH2 domain with a PDGF receptor phosphorylation site: structural features and analysis of conformational changes.

Circular dichroism and fluorescence spectroscopy were used to investigate the structure of the p85 alpha subunit of the PI 3-kinase, a closely related p85 beta protein, and a recombinant SH2 domain-containing fragment of p85 alpha. Significant spectral changes, indicative of a conformational change,...

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Detalhes bibliográficos
Main Authors: Panayotou, G, Bax, B, Gout, I, Federwisch, M, Wroblowski, B, Dhand, R, Fry, M J, Blundell, T L, Wollmer, A, Waterfield, M D
Formato: Artigo
Idioma:Inglês
Publicado em: 1992
Assuntos:
Research Article
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC556998/
https://ncbi.nlm.nih.gov/pubmed/1330535
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