Journal article
Solution structure studies of monomeric human TIP47/perilipin-3 reveal a highly extended conformation
Proteins, structure, function, and bioinformatics, v 80(8), pp 2046-2055
Aug 2012
PMID: 22508559
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Tail-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 homologue 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 β-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.
Metrics
Details
- Title
- Solution structure studies of monomeric human TIP47/perilipin-3 reveal a highly extended conformation
- Creators
- Robert M. G Hynson - School of Molecular Bioscience, The University of Sydney, NSW 2006, AustraliaCy M Jeffries - School of Molecular Bioscience, The University of Sydney, NSW 2006, AustraliaJill Trewhella - School of Molecular Bioscience, The University of Sydney, NSW 2006, AustraliaSimon Cocklin - Department of Biochemistry & Molecular Biology, Drexel University College of Medicine, Philadelphia, Pennsylvania 19102
- Publication Details
- Proteins, structure, function, and bioinformatics, v 80(8), pp 2046-2055
- Publisher
- Wiley
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000306132400011
- Scopus ID
- 2-s2.0-84863783823
- Other Identifier
- 991014877706504721
UN Sustainable Development Goals (SDGs)
This publication has contributed to the advancement of the following goals:
InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics