Structural highlights
Function
[SPTN1_RAT] Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane.
Publication Abstract from PubMed
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 A 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.
High-Resolution Crystal Structure of Spectrin SH3 Domain Fused with a Proline-Rich Peptide.,Gushchina LV, Gabdulkhakov AG, Nikonov SV, Filimonov VV J Biomol Struct Dyn. 2011 Dec;29(3):485-95. PMID:22066535[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gushchina LV, Gabdulkhakov AG, Nikonov SV, Filimonov VV. High-Resolution Crystal Structure of Spectrin SH3 Domain Fused with a Proline-Rich Peptide. J Biomol Struct Dyn. 2011 Dec;29(3):485-95. PMID:22066535
