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Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO
Published on: December 28, 2019
NMR-driven secondary and tertiary structure model of Ca2+-loaded calexcitin
Zoltan Gombos1, Kyoko L Yap, Mitsuhiko Ikura
1Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, Ont., Canada M5G 1L7. zoltan.gombos@nrc-cnrc.gc.ca
Abstract:
Calexcitin (CE) is a Ca2+-binding protein which is expressed in neuronal cells and is a member of the sarcoplasmic Ca2+-binding protein subfamily. The peptide backbone of Ca2+-CE has been assigned by NMR and it shows that CE is composed of nine alpha-helices-forming four EF-hands and an additional helix near the C-terminus. A structural model of CE suggests the presence of a putative recessed hydrophobic pocket that may be involved in Ca2+-mediated protein-ligand interactions. This feature is unique to CE and is absent in other SCPs, such as those from Branchiostoma and Nereis, and from calerythrin.
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