Solution structure of a fragment of the dimerization domain of E2F-1 determined by circular dichroism, 1H nuclear magnetic resonance and distance geometry.
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 alphaH 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.
Laboratory of Structure Biology, School of Life Science, University of Science and Technology of China, Hefei, Anhui, 230026, PR China.
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Guang
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Wu
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Tao
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Xia
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Shi
D000595:Amino Acid Sequence; D002352:Carrier Proteins; D018797:Cell Cycle Proteins; D002942:Circular Dichroism; D004268:DNA-Binding Proteins / Q000737:chemistry*; D019281:Dimerization; D050684:E2F Transcription Factors; D050687:E2F1 Transcription Factor; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D056465:Retinoblastoma-Binding Protein 1; D012996:Solutions; D014157:Transcription Factors / Q000737:chemistry*
D002352:Carrier Proteins; D018797:Cell Cycle Proteins; D004268:DNA-Binding Proteins; D050684:E2F Transcription Factors; D050687:E2F1 Transcription Factor; D010455:Peptides; D056465:Retinoblastoma-Binding Protein 1; D012996:Solutions; D014157:Transcription Factors