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Default Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain

Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain

March 2012
Publication year: 2012
Source:Biochimie, Volume 94, Issue 3



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) but neither the N-domain (N-BP-2) nor the linker domain have been characterised. Here we present NMR resonance assignments for human N-BP-2, achieved by recording spectra at low protein concentration using non-uniform sampling and maximum entropy reconstruction. Analysis of secondary chemical shifts shows that N-BP-2 possesses a secondary structure similar to that of other IGFBPs. Although aggregation hampered determination of the solution structure for N-BP-2, a homology model was generated based on the high degree of sequence and structure homology exhibited by the IGFBPs. This model was consistent with experimental NMR and SAXS data and displayed some unique features such as a Pro/Ala-rich non-polar insert, which formed a flexible solvent-exposed loop on the surface of the protein opposite to the IGF-binding interface. NMR data indicated that this loop could adopt either of two alternate conformations in solution – an entirely flexible conformation and one containing nascent helical structure. This loop and an adjacent poly-proline sequence may comprise a potential SH3 domain interaction site for binding to other proteins.
Highlights

? Determined NMR peak assignments for N-domain of human IGFBP-2 (N-BP-2). ? NMR data indicate N-BP-2 structure is similar to N-domain of other IGFBPs. ? N-BP-2 has a Pro/Ala-rich loop that differs from other IGFBPs. ? NMR data show that the loop adopts two distinct conformations. ? The loop is a potential SH3 domain binding site.





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