Secondary structure determination of 15N-labelled human Long-[Arg-3]-insulin-like growth factor 1 by multidimensional NMR spectroscopy

FEBS Letters
L G LaajokiM A Keniry

Abstract

Insulin-like growth factors (IGFs) are a group of proteins that promote cell growth and differentiation. Long-[Arg-3]-IGF-I (Francis et al. (1992) J. Mol. Endocrinol. 8, 213-223), a potent analogue of IGF-I, which has a Glu-3 to Arg-3 substitution and a hydrophobic, thirteen amino acid N-terminal extension, has been studied by 1H,15N NMR spectroscopy. All the backbone 1H and 15N assignments and most of the 1H sidechain assignments have been completed. The secondary structure elements were identified by determining the sequential and medium range NOEs from sensitivity-enhanced 15N-NOESY-HSQC and sensitivity-enhanced 15N-HSQC-NOESY-HSQC spectra. The IGF-I domain of Long-[Arg-3]-IGF-I was found to have an almost identical structure to IGF-I. The N-terminal seven amino acid residues of the extension have very few medium range or long range NOEs but the next five amino acids form a turn-like structure that is spatially close to the beginning of helix 1 in the IGF-I domain. Hydrogen-deuterium exchange experiments show that all the slowly exchanging backbone amide protons in the IGF-I domain are either in the helical or the extended structural elements. Many of the amide protons in the N-terminal extension are also protected from the ...Continue Reading

References

Jul 5, 1990·European Journal of Biochemistry·R E Humbel
May 1, 1989·The Biochemical Journal·C J BagleyJ C Wallace
Jan 1, 1985·Annual Review of Physiology·E R FroeschJ Zapf
Nov 1, 1983·Quarterly Reviews of Biophysics·S W Englander, N R Kallenbach
May 1, 1993·International Journal of Peptide and Protein Research·A SatoY Kobayashi
Jul 1, 1995·Journal of Biomolecular NMR·C BartelsK Wüthrich

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Citations

Dec 6, 2008·Growth Hormone & IGF Research : Official Journal of the Growth Hormone Research Society and the International IGF Research Society·Zhihe KuangRaymond S Norton
Apr 1, 2000·The Journal of Biological Chemistry·L G LaajokiM A Keniry

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