1H, 15N and 13C assignments of domain 5 of Dictyostelium discoideum gelation factor (ABP-120) in its native and 8M urea-denatured states
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The gelation factor from Dictyostelium discoideum (ABP-120) is an actin binding protein consisting of six immunoglobulin (Ig) domains in the C-terminal rod domain. We have recently used the pair of domains 5 and 6 of ABP-120 as a model system for studying multi-domain nascent chain folding on the ribosome. Here we present the NMR assignments of domain 5 in its native and 8M urea-denatured states.
KeywordsProtein folding Nascent chain Urea Ribosome ABP-120
STDH is a recipient of a Netherlands Ramsay and a Human Frontier Science Program Long-term Fellowship (LT0798/2005). LDC is a NH&MRC C.J. Martin Fellow. JC is a recipient of an HFSP Young Investigator’s Award (RGY67/2007). JC and CMD acknowledge funding from the Wellcome and Leverhulme Trusts. We thank Prof. Paola Fucini for providing the DNA plasmid of domains 5 and 6 of ABP-120 from which the current construct was derived, and the staff of the Biomolecular NMR Facility, Department of Chemistry, University of Cambridge.
- Goddard TD, Kneller DG Sparky 3. University of California: San Francisco. http://www.cgl.ucsf.edu/home/sparky/