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TitlePassenger sequences can promote interlaced dimers in a common variant of the maltose-binding protein.
Journal, issue, pagesSci Rep, Vol. 9, Page 20396-20396, Year 2019
Publish dateNov 26, 2019 (structure data deposition date)
AuthorsMomin, A.A. / Hameed, U.F.S. / Arold, S.T.
External linksSci Rep / PubMed:31892719
MethodsX-ray diffraction
Resolution2.004 - 3.2 Å
Structure data

PDB-6les:
3D domain-swapped dimer of the maltose-binding protein fused to a fragment of the focal adhesion kinase
Method: X-RAY DIFFRACTION / Resolution: 2.004 Å

PDB-6lf3:
3D domain-swapped dimer of the maltose-binding protein fused to a fragment of the protein-tyrosine kinase 2-beta
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli (strain k12) (bacteria)
  • homo sapiens (human)
KeywordsSUGAR BINDING PROTEIN / maltose binding protein / domain-swapping / arm exchange / folding / passenger protein / surface entropy reduction / fixed-arm carrier / dimer / FAK / apo-protein / PYK2

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