Structural basis of nSH2 regulation and lipid binding in PI3Kα

We report two crystal structures of the wild-type phosphatidylinositol 3-kinase α (PI3Kα) heterodimer refined to 2.9 Å and 3.4 Å resolution: the first as the free enzyme, the second in complex with the lipid substrate, diC4-PIP(2), respectively. The first structure shows key interactions of the N-te...

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Главные авторы: Miller, Michelle S., Schmidt-Kittler, Oleg, Bolduc, David M., Brower, Evan T., Chaves-Moreira, Daniele, Allaire, Marc, Kinzler, Kenneth W., Jennings, Ian G., Thompson, Philip E., Cole, Philip A., Amzel, L. Mario, Vogelstein, Bert, Gabelli, Sandra B.
Формат: Artigo
Язык:Inglês
Опубликовано: Impact Journals LLC 2014
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Priority Research Paper
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC4170646/
https://ncbi.nlm.nih.gov/pubmed/25105564
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