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Structure paper

TitleExchange, promiscuity, and orthogonality in de novo designed coiled-coil peptide assemblies.
Journal, issue, pagesChem Sci, Vol. 16, Page 1826-1836, Year 2025
Publish dateAug 8, 2024 (structure data deposition date)
AuthorsKurgan, K.W. / Martin, F.J.O. / Dawson, W.M. / Brunnock, T. / Orr-Ewing, A.J. / Woolfson, D.N.
External linksChem Sci / PubMed:39720134
MethodsX-ray diffraction
Resolution1.49 - 2.099 Å
Structure data

PDB-9gf2:
CC-Hex-hen2 variant peptide with Hendecad repeat substitution
Method: X-RAY DIFFRACTION / Resolution: 2.099 Å

PDB-9gf3:
CC-Hept-hen2 variant peptide with Hendecad repeat substitution
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-9gf4:
CC-Hept-IV-hen2 variant peptide with Hendecad repeat substitution
Method: X-RAY DIFFRACTION / Resolution: 1.49 Å

Chemicals

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

ChemComp-FMT:
FORMIC ACID

ChemComp-NA:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-NH4:
AMMONIUM ION

ChemComp-P33:
3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL / precipitant*YM

Source
  • synthetic construct (others)
KeywordsDE NOVO PROTEIN / Hendecad Repeat / Coiled-Coils / De novo Design / Coiled-Coil

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