Foldable subunits of helix protein.
Detection of foldable subunits in proteins is an important approach to understand their evolutions and find building motifs for de novo protein design. Using united-residue model, we simulated the folding of a six-helix protein with a length of 120 amino acids (C-terminal domain of Ku86). The folding behaviors, structural topology and sequence repetition of this protein all suggest that it may have a two-fold quasi-repetition or symmetry in its sequence and structure. Therefore, we simulated the folding of its two halves (1-60 and 61-120 amino acids) and find that they can fold into native conformations independently. It is also found that their folding behaviors are very similar to other three-helix bundles. This suggests that this protein may be divided into two foldable halves.
He
Yi
Y
Biomolecular Physics and Modeling Group, Department of Physics, Huazhong University of Science and Technology, Wuhan 430074, China.
Zhou
Rui
R
Huang
Yanzhao
Y
Xiao
Yi
Y
D000818:Animals; D034961:Antigens, Nuclear / Q000737:chemistry / Q000502:physiology*; D003198:Computer Simulation; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000502:physiology*; D000072200:Ku Autoantigen; D008958:Models, Molecular; D017510:Protein Folding; D021122:Protein Subunits / Q000737:chemistry / Q000502:physiology*
D034961:Antigens, Nuclear; D004268:DNA-Binding Proteins; D021122:Protein Subunits; D000072200:Ku Autoantigen