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The Interaction between PSD-95 and Ca2+/Calmodulin Is Enhanced by PDZ-Binding Proteins.
- Source :
-
Journal of Biochemistry . Aug2005, Vol. 138 Issue 2, p177-182. 6p. - Publication Year :
- 2005
-
Abstract
- In this study, we evaluate the interaction between the postsynaptic scaffolding protein, PSD-95, and calmodulin. Surface plasmon resonance spectroscopy was used to characterize the binding of PSD-95 to calmodulin that had been immobilized on a sensor chip. Additionally, soluble calmodulin was found to inhibit the binding of PSD-95 to immobilized calmodulin. The HOOK region of PSD-95, which is located between the src homology 3 domain and the guanylate kinase–like domain, was determined to be involved in the binding of PSD-95 to calmodulin. We also found that C-terminal peptides from proteins such as CRIPT and the N-methyl-d-aspartate receptor NR2B subunit, which associate with the PDZ domain of PSD-95, enhanced the affinity of PSD-95 for calmodulin. The binding of ligands to the PDZ domain may change the conformation of PSD-95 and affect the interaction between PSD-95 and calmodulin. [ABSTRACT FROM PUBLISHER]
Details
- Language :
- English
- ISSN :
- 0021924X
- Volume :
- 138
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 44543697
- Full Text :
- https://doi.org/10.1093/jb/mvi107