Structural highlights
Function
[SPTN1_CHICK] Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Here we present the high-resolution NMR structure of a chimera (SPCp41) between alpha-spectrin SH3 domain and the decapeptide p41. The tertiary structure mimics perfectly the interactions typically found in SH3-peptide complexes and is remarkably similar to that of the complex between the separate Spc-SH3 domain and ligand p41. Relaxation data confirm the tight binding between the ligand and SH3 part of the chimera. This chimera will serve as a tool for a deeper understanding of the relationship between structure and thermodynamics of binding using a combination of NMR, stability and site-directed mutagenesis studies, which can lead to an effective strategy for ligand design.
The high-resolution NMR structure of a single-chain chimeric protein mimicking a SH3-peptide complex.,Candel AM, Conejero-Lara F, Martinez JC, van Nuland NA, Bruix M FEBS Lett. 2007 Feb 20;581(4):687-92. Epub 2007 Jan 22. PMID:17275816[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Candel AM, Conejero-Lara F, Martinez JC, van Nuland NA, Bruix M. The high-resolution NMR structure of a single-chain chimeric protein mimicking a SH3-peptide complex. FEBS Lett. 2007 Feb 20;581(4):687-92. Epub 2007 Jan 22. PMID:17275816 doi:10.1016/j.febslet.2007.01.032
