1H, 13C and 15N resonance assignments of the GTPase-activating (GAP) and Ral binding domains (GBD) of RLIP76 (RalBP1)

RLIP76 (also known as RalBP1) is an effector for Ral small G proteins. RLIP76 is a multifunctional, multi-domain protein that includes a GTPase activating domain for the Rho family (RhoGAP domain) and a GTPase binding domain (GBD) for the Ral small G proteins. The juxtaposition of these two domains...

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Bibliographic Details
Published in:Biomolecular NMR assignments 2012-10, Vol.6 (2), p.119-122
Main Authors: Rajasekar, Karthik V., Campbell, Louise J., Nietlispach, Daniel, Owen, Darerca, Mott, Helen R.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
ATP-Binding Cassette Transporters - chemistry
Biochemistry
Biological and Medical Physics
Biophysics
Carbon Isotopes
GTPase-Activating Proteins - chemistry
Molecular Sequence Data
Nitrogen Isotopes
Nuclear Magnetic Resonance, Biomolecular
Physics
Physics and Astronomy
Polymer Sciences
Protein Structure, Secondary
Protein Structure, Tertiary
Protons
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Summary:RLIP76 (also known as RalBP1) is an effector for Ral small G proteins. RLIP76 is a multifunctional, multi-domain protein that includes a GTPase activating domain for the Rho family (RhoGAP domain) and a GTPase binding domain (GBD) for the Ral small G proteins. The juxtaposition of these two domains (GAP and GBD) may be a strategy employed to co-ordinate regulation of Rho family and Ral-controlled signalling pathways at a crossover node. Here we present the 1 H, 15 N and 13 C NMR backbone and sidechain resonance assignments of the GAP and GBD di-domain (31 kDa).
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-011-9337-y