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TitleA Conformation Selective Mode of Inhibiting SRC Improves Drug Efficacy and Tolerability.
Journal, issue, pagesCancer Res., Vol. 81, Page 5438-5450, Year 2021
Publish dateFeb 8, 2021 (structure data deposition date)
AuthorsTemps, C. / Lietha, D. / Webb, E.R. / Li, X.F. / Dawson, J.C. / Muir, M. / Macleod, K.G. / Valero, T. / Munro, A.F. / Contreras-Montoya, R. ...Temps, C. / Lietha, D. / Webb, E.R. / Li, X.F. / Dawson, J.C. / Muir, M. / Macleod, K.G. / Valero, T. / Munro, A.F. / Contreras-Montoya, R. / Luque-Ortega, J.R. / Fraser, C. / Beetham, H. / Schoenherr, C. / Lopalco, M. / Arends, M.J. / Frame, M.C. / Qian, B.Z. / Brunton, V.G. / Carragher, N.O. / Unciti-Broceta, A.
External linksCancer Res. / PubMed:34417202
MethodsX-ray diffraction
Resolution1.5 Å
Structure data

PDB-7ng7:
Src kinase bound to eCF506 trapped in inactive conformation
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-UCW:
tert-butyl (4-(4-amino-1-(2-(4-(dimethylamino)piperidin-1-yl)ethyl)-1H-pyrazolo[3,4-d]pyrimidin-3-yl)-2-methoxyphenyl)carbamate

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / Src kinase / inhibitor complex / inactive kinase

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