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 language||English (US)|
|Number of pages||12|
|Journal||Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology|
|State||Published - Oct 14 1998|
Bibliographical noteFunding Information:
We thank Dr. P. Guntert and Prof. K. Wuthrich for providing the programs PROSA, CALIBA, HABAS and DIANA. We thank Dr. C. Bartels and K. Wuthrich for providing XEASY. Special thanks to Dr. Q.G. Gong for his stimulating suggestions during this work. This work is supported by the Foundation of Chinese Academy of Science and the Chinese National Science Foundation.
Copyright 2007 Elsevier B.V., All rights reserved.
- Circular dichroism
- Coiled coil dimerization
- Distance geometry
- Nuclear magnetic resonance