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NMR resonance assignments of caspase recruitment domain of RIP2 kinase

NMR resonance assignments of caspase recruitment domain of RIP2 kinase Receptor interacting protein-2, RIP2, is a serine/threonine kinase and has sequence homology to RIP. It functions as an adaptor molecule for some members from the tumor necrosis factor receptor family and mediates divergent signaling pathways including NF-κB activation and cell death. RIP2 contains an N-terminal kinases domain and a C-terminal caspase activation and recruitment domain (CARD). The apoptotic activity of RIP2 is restricted to its C-terminal CARD domain while NF-κB activation requires the intact RIP2 for binding. RIP2 CARD involved homotypic or heterotypic interactions with members of the death domains superfamily. Here I report backbone and sidechain 1H, 13C and 15N resonance assignments of soluble RIP2 CARD as a basis for further structural and functional studies. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biomolecular NMR Assignments Springer Journals

NMR resonance assignments of caspase recruitment domain of RIP2 kinase

Biomolecular NMR Assignments , Volume 10 (2) – Mar 16, 2016

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References (17)

Publisher
Springer Journals
Copyright
Copyright © 2016 by Springer Science+Business Media Dordrecht
Subject
Physics; Biophysics and Biological Physics; Polymer Sciences; Biochemistry, general
ISSN
1874-2718
eISSN
1874-270X
DOI
10.1007/s12104-016-9675-x
pmid
26983939
Publisher site
See Article on Publisher Site

Abstract

Receptor interacting protein-2, RIP2, is a serine/threonine kinase and has sequence homology to RIP. It functions as an adaptor molecule for some members from the tumor necrosis factor receptor family and mediates divergent signaling pathways including NF-κB activation and cell death. RIP2 contains an N-terminal kinases domain and a C-terminal caspase activation and recruitment domain (CARD). The apoptotic activity of RIP2 is restricted to its C-terminal CARD domain while NF-κB activation requires the intact RIP2 for binding. RIP2 CARD involved homotypic or heterotypic interactions with members of the death domains superfamily. Here I report backbone and sidechain 1H, 13C and 15N resonance assignments of soluble RIP2 CARD as a basis for further structural and functional studies.

Journal

Biomolecular NMR AssignmentsSpringer Journals

Published: Mar 16, 2016

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