NDLI: Chemical shift assignments of calmodulin constructs with EF hand mutations

Content Provider	Springer Nature Link
Author	Piazza, Michael Guillemette, J. Guy Dieckmann, Thorsten
Copyright Year	2016
Abstract	Calmodulin (CaM) is a ubiquitous cytosolic Ca$^{2+}$-binding protein able to bind and regulate hundreds of different proteins. It consists of two globular domains joined by a flexible central linker region. Each one of these domains contains two EF hand pairs capable of binding to Ca$^{2+}$. Upon Ca$^{2+}$ binding CaM undergoes a conformational change exposing hydrophobic patches that interact with its intracellular target proteins. CaM is able to bind to target proteins in the Ca$^{2+}$-replete and Ca$^{2+}$-deplete forms. To study the Ca$^{2+}$-dependent/independent properties of binding and activation of target proteins by CaM, CaM constructs with Ca$^{2+}$ binding disrupting mutations of Asp to Ala at position one of each EF hand have been used. One target protein of CaM is nitric oxide synthase, which catalyzes the production of nitric oxide. At elevated Ca$^{2+}$ concentrations, CaM binds to neuronal NOS and endothelial NOS, making them the Ca$^{2+}$-dependent NOS enzymes. In contrast, inducible NOS is transcriptionally regulated in vivo and binds to CaM at basal levels of Ca$^{2+}$. Here we report the NMR backbone and sidechain resonance assignments of C-lobe Ca$^{2+}$-replete and deplete CaM$_{12}$, N-lobe Ca$^{2+}$-replete and deplete CaM$_{34}$, CaM$_{1234}$ in the absence of Ca$^{2+}$ and N-lobe Ca$^{2+}$-replete CaM$_{34}$ with the iNOS CaM-binding domain peptide.
Starting Page	193
Ending Page	198
Page Count	6
File Format	PDF
ISSN	18742718
Journal	Biomolecular NMR Assignments
Volume Number	10
Issue Number	1
e-ISSN	1874270X
Language	English
Publisher	Springer Netherlands
Publisher Date	2016-01-07
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Calmodulin Nitric oxide synthase NMR spectroscopy Resonance assignment Biophysics and Biological Physics Polymer Sciences Biochemistry
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biochemistry

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1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
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3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
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