Journal
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
Volume 29, Issue 3, Pages 485-495Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2011.10507400
Keywords
Chimeric protein; Spectrin SH3; Pro line-rich peptide; X-ray; Structure.
Categories
Funding
- RAS on Molecular and Cellular Biology
- Russian President Program for Young Scientists [MK-2917.2010.4]
- RFBR [03-04-48331]
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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 angstrom 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 twofold non-crystallographic axis and the ligand lies in two opposite orientations with respect to the conservative binding sites of SH3 domains.
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