Solution structure of a fragment of the dimerization domain of DP-1 determined by 1H-nuclear magnetic resonance and distance geometry

Shouhong Guang, Jihui Wu, Tianning Yu, Youlin Xia, Yunyu Shi

Research output: Contribution to journalArticlepeer-review


The structure of a synthesized peptide with the sequence of NHILPNESAYDQKNIRRRVYDALNVLMAMNIISK that corresponds to residues 151-184 of transcription factor DP-1 (Girling et al., Nature 362 (1993) 83-87) was determined by 1H-nuclear magnetic resonance in water and 40% d3-trifluoroethanol/water, respectively. Nuclear Overhauser effect cross peaks, αH chemical shifts and J-coupling constants of αH-NH show that the peptide consists a helix from Ser-8 to Ser-33 in solution. Fifty structures were constructed with 288 upper distance limits and 21 angle constraints by DIANA (Guntert et al., J. Mol. Biol. 217 (1991) 517-530). Although the N-terminal of the peptide exhibits a random conformation, the 20 best structures show a root mean square deviation of 0.89±0.36 A for backbone atoms and 1.80±0.34 A for heavy atoms from residue Ser-8 to Ser-33. This result supports the proposal that DP-1 and E2F-1 may dimerize with a coiled-coil type interaction. Copyright (C) 1998 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)18-28
Number of pages11
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Issue number1
StatePublished - Dec 8 1998


  • Coiled coil
  • DP-1
  • Dimerization
  • Distance geometry
  • NMR

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