TY - JOUR
T1 - Transient stability of the helical pattern of region F19-L22 of the N-terminal domain of p53
T2 - A molecular dynamics simulation study
AU - Espinoza-Fonseca, L. Michel
AU - Trujillo-Ferrara, José G.
N1 - Funding Information:
L.M.E.F would like to thank David D. Thomas for his support and encouragement. The authors’ research was supported by supercomputing time granted by the Minnesota Supercomputing Institute, University of Minnesota to L.M.E.F. and by grants from CONACYT and CGPI-IPN to J.G.T.F.
PY - 2006/4/28
Y1 - 2006/4/28
N2 - Two molecular dynamics simulations of the region E17-N29 of p53 (p53 17-29) at different temperatures were performed for a total time of 0.2 μs, to study the conformational landscape of this region. Previous studies have suggested that this region displays different structural motifs, such as helix of a double β-turn, and that its secondary structure might be transiently stable. Interestingly, in this study it was found that the region F19-L25, and particularly its fragment F19-L22, display a stable, transient helical pattern at sub-microsecond periods. The region F19-L22, which contains one of the most important residues needed for the interaction of p53 with MDM2, seems to be formed and stabilized by the existence of one hydrophobic and one aromatic cluster. The main function of these clusters is to help their surrounding area to desolvate, to allow the hydrogen bond network, therefore favoring the formation of a stable helix. This preliminary study would be useful for a better understanding of the structure and function of the N-terminal domain of p53 and its implications for the control of different types of cancer.
AB - Two molecular dynamics simulations of the region E17-N29 of p53 (p53 17-29) at different temperatures were performed for a total time of 0.2 μs, to study the conformational landscape of this region. Previous studies have suggested that this region displays different structural motifs, such as helix of a double β-turn, and that its secondary structure might be transiently stable. Interestingly, in this study it was found that the region F19-L25, and particularly its fragment F19-L22, display a stable, transient helical pattern at sub-microsecond periods. The region F19-L22, which contains one of the most important residues needed for the interaction of p53 with MDM2, seems to be formed and stabilized by the existence of one hydrophobic and one aromatic cluster. The main function of these clusters is to help their surrounding area to desolvate, to allow the hydrogen bond network, therefore favoring the formation of a stable helix. This preliminary study would be useful for a better understanding of the structure and function of the N-terminal domain of p53 and its implications for the control of different types of cancer.
KW - Folding
KW - Molecular dynamics simulations
KW - N-terminal domain
KW - p53
KW - p53-MDM2 interaction
UR - http://www.scopus.com/inward/record.url?scp=33645095919&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2006.02.129
DO - 10.1016/j.bbrc.2006.02.129
M3 - Artículo
C2 - 16530164
SN - 0006-291X
VL - 343
SP - 110
EP - 116
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -