Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin
β Scribed by Yamauchi, Emiko ;Nakatsu, Toru ;Matsubara, Mamoru ;Kato, Hiroaki ;Taniguchi, Hisaaki
- Book ID
- 109965436
- Publisher
- Nature Publishing Group
- Year
- 2003
- Tongue
- English
- Weight
- 300 KB
- Volume
- 10
- Category
- Article
- ISSN
- 1545-9993
- DOI
- 10.1038/nsb900
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## Abstract A 22βresidue synthetic peptide encompassing the calmodulin (CaM)βbinding domain of skeletal muscle myosin light chain kinase was studied by twoβdimensional NMR and CD spectroscopy. In water the peptide does not form any regular structure; however, addition of the helixβinducing solvent
Tb(III) luminescence is used to probe the conformational change induced in the calcium regulatory protein calmodulin upon binding to a target peptide. The luminescence lifetime for Tb(III) measured by frequency domain fluorimetry increases from 1278 microseconds for the calmodulin complex to 1496 mi