title: Theoretical structural insights into the snakin/GASA family.
abstract: Among the main classes of cysteine-stabilized antimicrobial peptides, the snakin/GASA family has not yet had any structural characterization. Through the combination of ab initio and comparative modeling with a disulfide bond predictor, the three-dimensional structure prediction of snakin-1 is reported here. The structure was composed of two long α-helices with a disulfide pattern of Cys(I)-Cys(IX), Cys(II)-Cys(VII), Cys(III)-Cys(IV), Cys(V)-Cys(XI), Cys(VI)-Cys(XII) and Cys(VIII)-Cys(X). The overall structure was maintained throughout molecular dynamics simulation. Snakin-1 showed a small degree of structural similarity with thionins and α-helical hairpins. This is the first report of snakin-1 structural characterization, shedding some light on the snakin/GASA family.
authors.affiliation: Centro de Análises Proteômicas e Bioquímicas, Pós-Graduação em Ciências Genômicas e Biotecnologia, Universidade Católica de Brasília, Brasília-DF, Brazil.
authors.forename: William F
authors.initials: WF
authors.lastname: Porto
authors.forename: Octavio L
authors.initials: OL
authors.lastname: Franco
mesh_terms: D000595:Amino Acid Sequence; D017124:Conserved Sequence; D003553:Cystine / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D020539:Sequence Analysis, Protein
chemical_list: D010940:Plant Proteins; C117071:SN1 protein, Solanum tuberosum; D003553:Cystine