Abstracts Keynote & Plenary

(Trichoplusia, ni) there was a dose and time dependent relationship between the protein express level
of CYP4L4 and concentration of fenvalerate, a potent synthetic pesticide, suggesting that CYP4L4 was
implicated in pesticide metabolism and resistance [1]. In this study a three-dimensional model structure
of CYP4L4 is build based on the CYP4L4 protein sequence of Mamestra brassicae using the
homology modeling method and refined by molecular dynamics simulation. Then the molecular
docking was performed on the model structure and the molecular of fenvalerate. The docking results
show that the molecular of fenvalerate was positioned in the pocket with the side of hydrophobic
residues and another side of hydrophilic residues. In addition, the channel to enter into the pocket of
CYP4L4 was identified in the complex with fenvalerate. According to the conformation of fenvalerate
binding with CYP4L4 predicted by molecular docking, the hydroxylation position of fenvalerate was
close to the heme, the prosthetic group of P450 enzyme, indicating the rationality of the predicted
conformation. These observations provided the atomic-level interpretation how CYP4L4 interacted
with the fenvalerate and the insights into the modification of pesticide to avoid the resistance.
[1] Fang, X., D. Huang, Z. Wang, C. Wan, T. Sun, W. Xu, C. Liu, P. Zhou, and Z. Qiao, Cell Biol
PO-0
and dynamic properties of a new amyloidogenic chicken cystatin mutant I108T
University, 66 Chongshan Zhong Road, 110036 Shenyang, China
variant I108T is a mutant in the hydrophobic core of the molecule. It has shown many
Keyw
[1] Engh, D. Musil, U. Thiele, R. Huber, A.Karshikovl, J. Brzin, J. Kos and V. Turk,
[2] 2000, 7, 70–79.
akami and A. Kato, Protein Sci. 2006, 15,
C. Kutzner, D. van der Spoel and E. Lindahl, J. Chem. Theory Comput. 2008, 4, 435-447.
ng BspQI Nicking Enzymes and Application of N.BspQI in DNA Labeling and
oo 1
, James C. Samuelson 1
, Siu-Hong Chan 1
, Tamas Vincze 1
Toxicol. 2007, 23, 445.
27
Structural
Yuanyuan Yu1, Youtao Song1, 2
1. College of Life Science, Liaoning
2.Province Key Laboratory of Animal Resource and Epidemic Disease Prevention, 110036 Shenyang,
China
Chicken cystatin
amyloid-prone characteristics in our previous experimental study. To explore the detailed
structural and dynamic properties of the amyloidogenic mutant I108T, 10 ns molecular dynamic
simulations of the I108T mutant and wild-type chicken cystatins were performed in this study.
Our results suggested that the I108T mutant, which exhibited larger secondary structural
fluctuations and hydrophobic core expanding tendency compared with the wild-type chicken
cystatin, is a new amyloidogenic form of chicken cystatin, and therefore supported the hypothesis
to some extent that site mutations in the hydrophobic core might induce the domain swapping.
ords: Chicken cystatin, Molecular dynamic simulation, Amyloidosis, hydrophobic core, domain
swapping.
W. Bode, R.
EMBO J. 1988, 7, 2593 – 2599.
I. Olafsson and A. Grubb, Amyloid.
[3] J.W. He, Y.T. Song, N. Ueyama, A. Saito, H. Az
213-222.
[4] B. Hess,
PO-028
Engineeri
Production ofSingle-strand DNA
Penghua Zhang ,
pswich, MA 01938
1
, Priscilla Hiu-Mei T
Stephanie Doucette 1
, Stefan Bäckström 2
, Konstantinos D. Potamousis 3
, Timothy M. Schramm 3
, Dan
Forrest 3
, David C. Schwartz 3
, Shuang-yong Xu1 *
1. New England Biolabs, Inc. 240 County Road, I