1H, 15N, 13C resonance assignment of 9.7 M urea-denatured state of the GTPase effector domain (GED) of dynamin.
The GTPase effector domain (GED) of dynamin, a multi-domain protein involved in endocytosis, forms a megadalton-sized self-assembly (even at micromolar concentrations) in native conditions in vitro. While such large assemblies have remained inaccessible to detailed NMR structural characterization, till date, a significant recent achievement has been the elucidation of the GED association pathway starting from a Gdn-HCl denatured monomer. Since, the nature of the denaturant has a strong influence on the conformational preferences in the denatured states, and hence on the association pathways, or even on the final assembly, we report here the NMR resonance assignment of 9.7 M urea-denatured GED from Homo sapiens. This will form the basis for the characterization of the association pathways and the final assembly driven by urea dilution.
Chugh
Jeetender
J
Department of Chemical Sciences, Tata Institute of Fundamental Research, 1, Homi Bhabha Road, Mumbai, 400005, India.
Sharma
Shilpy
S
Kumar
Dinesh
D
Hosur
Ramakrishna V
RV
D002247:Carbon Isotopes / Q000737:chemistry; D034281:Dynamins / Q000737:chemistry*; D020558:GTP Phosphohydrolases / Q000737:chemistry*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D009587:Nitrogen Isotopes / Q000737:chemistry; D011489:Protein Denaturation; D017434:Protein Structure, Tertiary; D011522:Protons; D014508:Urea / Q000737:chemistry*
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons; D014508:Urea; D020558:GTP Phosphohydrolases; D034281:Dynamins