Journal article
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain
CA Galea, M Mobli, KA McNeil, TD Mulhern, JC Wallace, GF King, BE Forbes, RS Norton
Biochimie | Published : 2012
Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to -6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In addition to regulating IGF actions, IGFBPs have IGF-independent functions. IGFBP-2, the largest member of this family, is over-expressed in many cancers and has been proposed as a possible target for the development of novel anti-cancer therapeutics. The IGFBPs have a common architecture consisting of conserved N- and C-terminal domains joined by a variable linker domain. The solution structure and dynamics of the C-terminal domain of human IGFBP-2 have been reported (Kuang Z. et al. J. Mol. Biol. 364, 690-704, 2006) bu..
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Awarded by Australian Research Council
Funding Acknowledgements
We thank Gary Shooter and Zee Upton for valuable discussions and acknowledge support received from the staff and facilities of the Queensland NMR Network (QNN). This work was supported in part by grants from the Australian Research Council (LP0776825) and the National Health and Medical Research Council, Australia (Program grant 461219), as well as by Tissue Therapies Ltd. R.S.N. acknowledges fellowship support from NHMRC. This research was partly undertaken on the SAXS/WAXS beamline at the Australian Synchrotron, Victoria, Australia; we thank Dr Nigel Kirby and the other beamline staff for their assistance.