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 language||English (US)|
|Number of pages||11|
|Journal||Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology|
|State||Published - Dec 8 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. Wutrhich 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 Chinese National Science Foundation.
Copyright 2015 Elsevier B.V., All rights reserved.
- Coiled coil
- Distance geometry