title: High-resolution crystal structure of spectrin SH3 domain fused with a proline-rich peptide.
abstract: A new chimeric protein, named WT-CIIA, was designed by connecting the proline-rich decapeptide PPPVPPYSAG to the C-terminus of the alpha-spectrin SH3 domain through a natural twelve-residue linker to obtain a single-chain model that would imitate intramolecular SH3-ligand interaction. The crystal structure of this fusion protein was determined at 1.7 Å resolution. The asymmetric unit of the crystal contained two SH3 globules contacting with one PPPVPPY fragment located between them. The domains are related by the two-fold non-crystallographic axis and the ligand lies in two opposite orientations with respect to the conservative binding sites of SH3 domains.
authors: Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.
authors: Liubov V
authors: LV
authors: Gushchina
authors: Azat G
authors: AG
authors: Gabdulkhakov
authors: Stanislav V
authors: SV
authors: Nikonov
authors: Vladimir V
authors: VV
authors: Filimonov
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011392:Proline / Q000737:chemistry*; D017510:Protein Folding; D013049:Spectrin / Q000737:chemistry* / Q000378:metabolism; D018909:src Homology Domains
chemical_list: D008024:Ligands; D010455:Peptides; D013049:Spectrin; D011392:Proline