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Structure paper

TitleEngineered synthetic antibodies as probes to quantify the energetic contributions of ligand binding to conformational changes in proteins.
Journal, issue, pagesJ. Biol. Chem., Vol. 293, Page 2815-2828, Year 2018
Publish dateSep 12, 2017 (structure data deposition date)
AuthorsMukherjee, S. / Griffin, D.H. / Horn, J.R. / Rizk, S.S. / Nocula-Lugowska, M. / Malmqvist, M. / Kim, S.S. / Kossiakoff, A.A.
External linksJ. Biol. Chem. / PubMed:29321208
MethodsX-ray diffraction
Resolution1.95 - 2.6 Å
Structure data

PDB-5bjz:
Crystal structure of maltose binding protein in complex with an allosteric synthetic antibody
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-5bk1:
Crystal structure of maltose binding protein in complex with an endosteric synthetic antibody
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-5bk2:
Crystal structure of maltose binding protein in complex with a peristeric synthetic antibody
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-EPE:
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH buffer*YM

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

Source
  • escherichia coli o157:h7 (bacteria)
  • homo sapiens (human)
  • escherichia coli (E. coli)
KeywordsSUGAR BINDING PROTEIN / Maltose binding protein / conformation specific synthetic antibody / Fab fragment

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