Role of the linker domain and the 203-214 N-terminal residues in the human topoisomerase I DNA complex dynamics.

ABSTRACT: The influence of the N-terminal residues 203-214 and the linker domain on motions in the human topoisomerase I-DNA complex has been investigated by comparing the molecular dynamics simulations of the system with (topo70) or without (topo58/6.3) these regions. Topo58/6.3 is found to fluctuate more than topo70, indicating that the presence of the N-terminal residues and the linker domain dampen the core and C-terminal fluctuations. The simulations also show that residues 203-207 and the linker domain participate in a network of correlated movements with key regions of the enzyme, involved in the human topoisomerase I catalytic cycle, providing a structural-dynamical explanation for the better DNA relaxation activity of topo70 when compared to topo58/6.3. The data have been examined in relati

SUBMITTER: Chillemi G 

PROVIDER: S-EPMC1304917 | biostudies-literature | 2004 Dec

REPOSITORIES: biostudies-literature