期刊
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
卷 40, 期 2, 页码 612-621出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2020.1819419
关键词
Mx protein; polymorphism; molecular dynamics simulation; essential dynamics; interdomain motion; residue networks
资金
- Next-Generation Biogreen 21 Program, Rural Development Administration, Republic of Korea [PJ013151, PJ01324201]
- National Research Foundation of Korea [NRF-2018R1C1B6008141]
In this study, computational methods were used to investigate the structure and dynamics of wild-type and mutant chMx proteins. The results revealed differences in structure and stalk domain conformation between the wild-type and mutant proteins, which may be associated with the mutant's antiviral activity.
Myxovirus resistance (Mx) proteins are antiviral GTPases induced by type I interferons (IFNs). In chickens, a single Mx protein variant, S631N, has been suggested to possess antiviral activity. However, the impact of this variant on chicken Mx (chMx) protein structure and conformation has not been investigated. Hence, in this study, we applied computational methods such as molecular modeling, molecular dynamic simulation, inter domain motion and residue networks to examine the structure and dynamic behavior of wild-type and mutant chMx. At first, we built 3-dimensional structural models for both wild-type and mutant chMx proteins, which revealed that the structural organization of chMx was similar to that of human Mx proteins. Subsequently, molecular dynamics simulations revealed that angle variation around the hinge1 region led to the different stalk domain conformations between the wild-type and mutant chMx proteins. Domain motion analysis further suggested that the conformational differences in the loop region surrounded by the mutant residue may lead to an inclined stalk domain conformation in the mutant compared to the wild-type protein. In addition, we performed betweenness centrality analysis from residue interaction networks, to identify the crucial residues for intramolecular signal flow in chMx. The results of this study provided information on the differences in structure and dynamics between wild-type and mutant chMx, which may aid in understanding the structural features of the S631N mutant, that may be associated with chMx protein antiviral activity.
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