Author: Lang, Dorothy M.; Zemla, A. T.; Zhou, C. L. Ecale
Title: Highly similar structural frames link the template tunnel and NTP entry tunnel to the exterior surface in RNA-dependent RNA polymerases Document date: 2012_12_25
ID: s90geszi_99
Snippet: The structurally aligned sequences that comprise hmC are shown in Figure 6A . Motif C is the only RdRp motif that is not a component of a larger homomorphic structure. The segments immediately adjacent to both flanks of Motif C do not even cluster into subgroups. Motif C is short-12 residues in most RdRps and folds sharply back on itself ( Figure 6B ). The highly conserved residues (labeled Motif C) are at the surface of the template tunnel and b.....
Document: The structurally aligned sequences that comprise hmC are shown in Figure 6A . Motif C is the only RdRp motif that is not a component of a larger homomorphic structure. The segments immediately adjacent to both flanks of Motif C do not even cluster into subgroups. Motif C is short-12 residues in most RdRps and folds sharply back on itself ( Figure 6B ). The highly conserved residues (labeled Motif C) are at the surface of the template tunnel and both the N-terminal and C-terminal residues are at the exterior surface of the protein ( Figure 6C ).
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