High-Resolution Crystal Structure of Spectrin SH3 Domain Fused with a Proline-Rich Peptide
| Autor: | Azat Gabdulkhakov, Liubov V. Gushchina, Vladimir V. Filimonov, Stanislav Nikonov |
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| Rok vydání: | 2011 |
| Předmět: |
Models
Molecular Protein Folding Proline Molecular Sequence Data Protein domain Peptide macromolecular substances Crystal structure Crystallography X-Ray Ligands SH3 domain src Homology Domains Structural Biology Spectrin Amino Acid Sequence Proline rich Molecular Biology chemistry.chemical_classification Binding Sites Chemistry General Medicine Fusion protein Crystallography Peptides Linker |
| Zdroj: | Journal of Biomolecular Structure and Dynamics. 29:485-495 |
| ISSN: | 1538-0254 0739-1102 |
| DOI: | 10.1080/07391102.2011.10507400 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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