title: The role of glycine residues at the C-terminal peptide segment in antinociceptive activity: a molecular dynamics simulation.
abstract: Elucidating structural determinants in the functional regions of toxins can provide useful knowledge for designing novel analgesic peptides. Glycine residues at the C-terminal region of the neurotoxin BmK AGP-SYPU2 from the scorpion Buthus martensii Karsch (BmK) have been shown to be crucial to its analgesic activity. However, there has been no research on the structure-function relationship between the C-terminal segment of this toxin and its analgesic activity. To address this issue, we performed three MD simulations: one on the native structure and the other two on mutants of that structure. Results of these calculations suggest that the existence of glycine residues at the C-terminal segment stabilizes the protruding topology of the NC domain, which is considered an important determinant of the analgesic activity of BmK AGP-SYPU2.
authors.affiliation: School of Life Science and Bio-pharmaceutics, Shenyang Pharmaceutical University, Shenyang, Liaoning Province 110016, People's Republic of China.
authors.forename: Yong-Shan
authors.initials: YS
authors.lastname: Zhao
authors.forename: Rong
authors.initials: R
authors.lastname: Zhang
authors.forename: Yang
authors.initials: Y
authors.lastname: Xu
authors.forename: Yong
authors.initials: Y
authors.lastname: Cui
authors.forename: Yan-Feng
authors.initials: YF
authors.lastname: Liu
authors.forename: Yong-Bo
authors.initials: YB
authors.lastname: Song
authors.forename: Hong-Xing
authors.initials: HX
authors.lastname: Zhang
authors.forename: Jing-Hai
authors.initials: JH
authors.lastname: Zhang
mesh_terms: D000595:Amino Acid Sequence; D000700:Analgesics / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D005998:Glycine / Q000737:chemistry*; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D009154:Mutation; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012604:Scorpion Venoms / Q000737:chemistry* / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D000700:Analgesics; C551460:KAGAP protein, Buthus martensii Karsch; D010455:Peptides; D012604:Scorpion Venoms; D005998:Glycine