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-Structure paper
Title | Functional evolution of IGF2:IGF2R domain 11 binding generates novel structural interactions and a specific IGF2 antagonist. |
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Journal, issue, pages | Proc. Natl. Acad. Sci. USA, Vol. 113, Page E2766-E2775, Year 2016 |
Publish date | Mar 27, 2013 (structure data deposition date) |
Authors | Frago, S. / Nicholls, R.D. / Strickland, M. / Hughes, J. / Williams, C. / Garner, L. / Surakhy, M. / Maclean, R. / Rezgui, D. / Prince, S.N. ...Frago, S. / Nicholls, R.D. / Strickland, M. / Hughes, J. / Williams, C. / Garner, L. / Surakhy, M. / Maclean, R. / Rezgui, D. / Prince, S.N. / Zaccheo, O.J. / Ebner, D. / Sanegre, S. / Yu, S. / Buffa, F.M. / Crump, M.P. / Hassan, A.B. |
External links | Proc. Natl. Acad. Sci. USA / PubMed:27140600 |
Methods | NMR (solution) / X-ray diffraction |
Resolution | 2.8 Å |
Structure data | PDB-2m68: PDB-2m6t: PDB-5iei: |
Chemicals | ChemComp-GOL: ChemComp-EDO: ChemComp-SO4: |
Source |
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Keywords | ANTITUMOR PROTEIN / antitumor / directed evolution / high affinity / directed evolution and high affinity / TRANSPORT PROTEIN / IGF2 / IGF2R / domain 11 |