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Journal article
NMR structural characterization of the penta-peptide calpain inhibitor
FEBS Letters, Vol.583, pp.135-140
583
2009
PMID: 19059407
Web of Science ID: WOS:000261949200024
Abstract
Calpains are ubiquitous intracellular calcium- and thiol-dependent proteases. Their over activation, resulting in the degradation of various substrates, has been implicated in a number of cardiovascular and neurological disorders. Here, we present the first structural characterization of LSEAL pentapeptide, a potent calpain inhibitor, bound to the calmodulin-like domain of calpain. Our in vitro binding data supports the idea that domains other than calpain’s active site may be suitable targets for future development of therapeutic agents to be used to treat heart attack, traumatic brain injuries or a variety of neurodegenerative conditions, such as ischemic stroke.
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Details
- Title
- NMR structural characterization of the penta-peptide calpain inhibitor
- Publication Details
- FEBS Letters, Vol.583, pp.135-140
- Resource Type
- Journal article
- Publisher
- John Wiley & Sons Ltd.; United Kingdom
- Series
- 583
- Copyright
- 2008 Federation of European Biochemical Societies
- Identifiers
- WOS:000261949200024; 99380090784506600
- Academic Unit
- Hal Marcus College of Science and Engineering ; Biology
- Language
- English