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Structure paper

TitleThe Phe-Ile Zipper: A Specific Interaction Motif Drives Antiparallel Coiled-Coil Hexamer Formation.
Journal, issue, pagesBiochemistry, Vol. 56, Page 5300-5308, Year 2017
Publish dateMay 16, 2017 (structure data deposition date)
AuthorsSpencer, R.K. / Hochbaum, A.I.
External linksBiochemistry / PubMed:28876052
MethodsX-ray diffraction
Resolution2.023 - 2.201 Å
Structure data

PDB-5vte:
Hetero antiparallel coiled coil hexamer formed by de novo peptides
Method: X-RAY DIFFRACTION / Resolution: 2.023 Å

PDB-5w0j:
Antiparallel coiled coil hexamer formed by de novo peptides (ACC-Hex2).
Method: X-RAY DIFFRACTION / Resolution: 2.201 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

Source
  • synthetic construct (others)
KeywordsDE NOVO PROTEIN / antiparallel / hexamer / de novo / phe-ile zipper

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