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TitleCircumventing the stability-function trade-off in an engineered FN3 domain.
Journal, issue, pagesProtein Eng. Des. Sel., Year 2016
Publish dateApr 6, 2016 (structure data deposition date)
AuthorsPorebski, B.T. / Conroy, P.J. / Drinkwater, N. / Schofield, P. / Vazquez-Lombardi, R. / Hunter, M.R. / Hoke, D.E. / Christ, D. / McGowan, S. / Buckle, A.M.
External linksProtein Eng. Des. Sel. / PubMed:27578887
MethodsX-ray diffraction
Resolution2.46 - 2.535 Å
Structure data

PDB-5j7c:
A picomolar affinity FN3 domain in complex with hen egg-white lysozyme
Method: X-RAY DIFFRACTION / Resolution: 2.535 Å

PDB-5j7k:
Loop grafting onto a highly stable FN3 scaffold
Method: X-RAY DIFFRACTION / Resolution: 2.46 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
  • gallus gallus (chicken)
  • synthetic construct (others)
Keywordsprotein binding/hydrolase / Yeast surface display / high affinity / fibronectin type III / FN3 / protein binding-hydrolase complex / PROTEIN BINDING / loop grafting / rational design

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