Solution structure of a fragment of the dimerization domain of E2F-1 determined by circular dichroism, 1H nuclear magnetic resonance and distance geometry

Shouhong Guang, Jihui Wu, Limei Tao, Youlin Xia, Yunyu Shi

Research output: Contribution to journalArticle

Abstract

The structure of a synthesized peptide with the sequence GVVDLNWAAEVLKVQKRRIYDITNVLEGIQ which corresponds to residues 149-178 of transcription factor E2F-1 was determined by 1H nuclear magnetic resonance in 40% d3-TFE/water. NOE cross peaks and αH chemical shifts indicate that the peptide consists of a helix from Ala-8 to Leu-26 in this solution. Circular dichroism measurements confirm the presence of nearly 45% helix in TFE/water solution but show no evidence of helicity in water solution of this peptide. Fifty structures were constructed with 329 upper distance limits by DIANA. The 20 best conformers show a RMSD of 0.78 A for backbone atoms and 1.78 A for heavy atoms from residue Ala-8 to Leu-26. This result, together with our previous work on the solution structure of a fragment of DP-1, supports the proposal that E2F-1 and DP-1 may dimerize with a coiled-coil type interaction. Copyright (C) 1998 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)111-122
Number of pages12
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1388
Issue number1
DOIs
StatePublished - Oct 14 1998

Keywords

  • Circular dichroism
  • Coiled coil dimerization
  • Distance geometry
  • E2F-1
  • Nuclear magnetic resonance

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