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Title: High-resolution crystal structure of spectrin SH3 domain fused with a proline-rich peptide. Author: Gushchina LV, Gabdulkhakov AG, Nikonov SV, Filimonov VV. Journal: J Biomol Struct Dyn; 2011 Dec; 29(3):485-95. PubMed ID: 22066535. 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.[Abstract] [Full Text] [Related] [New Search]