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Simulation Study for Wild-Type and C101F Mutant of LIM2 Domain in FHL1

Myopathy is a rare disease lacking a fundamental therapy. Several genetic factors are involved in myopathy; those caused by mutations in FHL1 are rare. We performed molecular dynamics simulation of the LIM2 domain in FHL1 (four and a half LIM domain protein 1). We simulated a partial system consisting of only the LIM2 domain for the wild-type and C101F mutant to confirm the structural stability. We found that structural changes and fluctuations were larger for the mutant type than for the wild-type. Therefore, mutant type structures are unstable in water when the mutations are in residues constituting the zinc finger. Similar results were observed in the simulation of the LIM1+LIM2 domain.