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TitleStructural basis of an engineered dual-specific antibody: conformational diversity leads to a hypervariable loop metal-binding site.
Journal, issue, pagesProtein Eng. Des. Sel., Vol. 27, Page 391-397, Year 2014
Publish dateFeb 26, 2014 (structure data deposition date)
AuthorsFanning, S.W. / Walter, R. / Horn, J.R.
External linksProtein Eng. Des. Sel. / PubMed:25143596
MethodsX-ray diffraction
Resolution1.5 - 1.75 Å
Structure data

PDB-4pou:
VHH-metal in Complex with RNase A
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-4poy:
Engineered Dual Specific VHH antibody
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-4ppt:
Engineered Dual Specific VHH Antibody in Complex with a Nickel (II) Ion
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-NI:
NICKEL (II) ION

ChemComp-SO4:
SULFATE ION

Source
  • lama glama (llama)
  • bos taurus (cattle)
KeywordsHydrolase/Immune System / Hydrolase-Immune System complex / IMMUNE SYSTEM / Single domain antibody / VHH / Metalloregulation / Bispecific / Dual-Function / Protein Engineering / Affinity Control / Protein-Switch / Antibody Engineering / Nickel Binding Protein / Protein-Metal Coordination Geometry / Loop Dynamics / Protein Flexibility / Conformational Dynamics / Binding Thermodynamics / Antibody-metal Complex

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