TY - JOUR
T1 - A molecular dynamics study and free energy analysis of complexes between the Mlc1p protein and two IQ motif peptides
AU - Ganoth, Assaf
AU - Friedman, Ran
AU - Nachliel, Esther
AU - Gutman, Menachem
N1 - Funding Information:
This research is supported by the Israel Science Foundation (grant No. 427/01-1) and the United States-Israel Bi-National Science Foundation (grant No. 2002129). R.F. acknowledges the Colton Foundation for its support through the Colton Scholarship.
PY - 2006/10
Y1 - 2006/10
N2 - The Mlc1p protein from the budding yeast Saccharomyces cerevisiae is a Calmodulin-like protein, which interacts with IQ-motif peptides located at the yeast's myosin neck. In this study, we report a molecular dynamics study of the Mlc1p-IQ2 protein-peptide complex, starting with its crystal structure, and investigate its dynamics in an aqueous solution. The results are compared with those obtained by a previous study, where we followed the solution structure of the Mlc1p-IQ4 protein-peptide complex by molecular dynamics simulations. After the simulations, we performed an interaction free-energy analysis using the molecular mechanics Poisson-Boltzmann surface area approach. Based on the dynamics of the Mlc1p-IQ protein-peptide complexes, the structure of the light-chain-binding domain of myosin V from the yeast S. cerevisiae is discussed.
AB - The Mlc1p protein from the budding yeast Saccharomyces cerevisiae is a Calmodulin-like protein, which interacts with IQ-motif peptides located at the yeast's myosin neck. In this study, we report a molecular dynamics study of the Mlc1p-IQ2 protein-peptide complex, starting with its crystal structure, and investigate its dynamics in an aqueous solution. The results are compared with those obtained by a previous study, where we followed the solution structure of the Mlc1p-IQ4 protein-peptide complex by molecular dynamics simulations. After the simulations, we performed an interaction free-energy analysis using the molecular mechanics Poisson-Boltzmann surface area approach. Based on the dynamics of the Mlc1p-IQ protein-peptide complexes, the structure of the light-chain-binding domain of myosin V from the yeast S. cerevisiae is discussed.
UR - http://www.scopus.com/inward/record.url?scp=33749447306&partnerID=8YFLogxK
U2 - 10.1529/biophysj.106.085399
DO - 10.1529/biophysj.106.085399
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AN - SCOPUS:33749447306
SN - 0006-3495
VL - 91
SP - 2436
EP - 2450
JO - Biophysical Journal
JF - Biophysical Journal
IS - 7
ER -