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TitleMechanistic analysis of allosteric and non-allosteric effects arising from nanobody binding to two epitopes of the dihyrofolate reductase of Escherichia coli.
Journal, issue, pagesBiochim. Biophys. Acta, Vol. 1834, Page 2147-2157, Year 2013
Publish dateApr 5, 2012 (structure data deposition date)
AuthorsOyen, D. / Wechselberger, R. / Srinivasan, V. / Steyaert, J. / Barlow, J.N.
External linksBiochim. Biophys. Acta / PubMed:23911607
MethodsX-ray diffraction
Resolution1.75 - 2.8 Å
Structure data

PDB-4eig:
CA1698 camel antibody fragment in complex with DHFR
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-4eiz:
Structure of Nb113 bound to apoDHFR
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-4ej1:
Binding of Nb113 camelid antibody fragment with the binary DHFR:folate complex
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-4fhb:
Enhancing DHFR catalysis by binding of an allosteric regulator nanobody (Nb179)
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-FOL:
FOLIC ACID

ChemComp-PO4:
PHOSPHATE ION

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

Source
  • escherichia coli (E. coli)
  • lama glama (llama)
KeywordsOXIDOREDUCTASE/IMMUNE SYSTEM / NADP binding / OXIDOREDUCTASE-IMMUNE SYSTEM complex / FOLATE / Oxidoreductase/protein binding / Nanobody / Dihydrofolate reductase / Allosteric activator / Reductase / Oxidoreductase-protein binding complex

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