Solution structure studies of monomeric human TIP47/perilipin-3 reveal a highly extended conformation

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dc.contributor.authorHynson, RMGen_AU
dc.contributor.authorJeffries, CMen_AU
dc.contributor.authorTrewhella, Jen_AU
dc.contributor.authorCocklin, Sen_AU
dc.date.accessioned2014-10-13T01:11:45Zen_AU
dc.date.available2014-10-13T01:11:45Zen_AU
dc.date.issued2012-04-17en_AU
dc.date.statistics2014-10-13en_AU
dc.description.abstractTail-interacting protein of 47 kDa (TIP47) has two putative functions: lipid biogenesis and mannose 6-phosphate receptor recycling. Progress in understanding the molecular details of these two functions has been hampered by the lack of structural data on TIP47, with a crystal structure of the C-terminal domain of the mouse homolog constituting the only structural data in the literature so far. Our studies have first provided a strategy to obtain pure monodisperse preparations of the full-length TIP47/perilipin-3 protein, as well as a series of N-terminal truncation mutants with no exogenous sequences. These constructs have then enabled us to obtain the first structural characterization of the full-length protein in solution. Our work demonstrates that the N-terminal region of TIP47/perilipin-3, in contrast to the largely helical C-terminal region, is predominantly beta-structure with turns and bends. Moreover, we show that full-length TIP47/perilipin-3 adopts an extended conformation in solution, with considerable spatial separation of the N- and C-termini that would likely translate into a separation of functional domains. Proteins 2012;. © 2012, Wiley-Blackwell.en_AU
dc.identifier.citationHynson, R. M. G., Jeffries, C. M., Trewhella, J., & Cocklin, S. (2012). Solution structure studies of monomeric human TIP47/perilipin-3 reveal a highly extended conformation. Proteins: Structure, Function, and Bioinformatics, 80(8), 2046-2055. doi:10.1002/prot.24095en_AU
dc.identifier.govdoc4638en_AU
dc.identifier.issn0887-3585en_AU
dc.identifier.issue8en_AU
dc.identifier.journaltitleProteins: Structure, Function, and Bioinformaticsen_AU
dc.identifier.pagination2046-2055en_AU
dc.identifier.urihttp://dx.doi.org/10.1002/prot.24095en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/5910en_AU
dc.identifier.volume80en_AU
dc.language.isoenen_AU
dc.publisherWileyen_AU
dc.subjectDichroismen_AU
dc.subjectLight scatteringen_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectCrystal structureen_AU
dc.subjectLipidsen_AU
dc.subjectProteinsen_AU
dc.titleSolution structure studies of monomeric human TIP47/perilipin-3 reveal a highly extended conformationen_AU
dc.typeJournal Articleen_AU
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