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

doi:10.1016/S0167-4838(98)00171-X

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

Minnesota NMR Center

Research output: Contribution to journal › Article › peer-review

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 language	English (US)
Pages (from-to)	111-122
Number of pages	12
Journal	Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume	1388
Issue number	1
DOIs	https://doi.org/10.1016/S0167-4838(98)00171-X
State	Published - Oct 14 1998

Bibliographical note

Funding 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.

Keywords

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

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Solution structure of a fragment of the dimerization domain of E2F-1 determined by circular dichroism, ¹H nuclear magnetic resonance and distance geometry. / Guang, Shouhong; Wu, Jihui; Tao, Limei et al.
In: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, Vol. 1388, No. 1, 14.10.1998, p. 111-122.

Research output: Contribution to journal › Article › peer-review

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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.",

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