Nuclear magnetic resonance assignment and secondary structure of an ankyrin-like repeat-bearing protein: myotrophin

Protein Science : a Publication of the Protein Society
Y YangJ Qin

Abstract

Multidimensional heteronuclear NMR has been applied to the structural analysis of myotrophin, a novel protein identified from spontaneously hypertensive rat hearts and hypertrophic human hearts. Myotrophin has been shown to stimulate protein synthesis in myocytes and likely plays an important role in the initiation of cardiac hypertrophy, a major cause of mortality in humans. Recent cDNA cloning revealed that myotrophin has 11B amino acids containing 2.5 contiguous ANK repeats, a motif known to be involved in a wide range of macromolecular recognition. A series of two- and three-dimensional heteronuclear bond correlation NMR experiments have been performed on uniformly 15N-labeled or uniformly 15N/13C-labeled protein to obtain the 1H, 15N, and 13C chemical shift assignments. The secondary structure of myotrophin has been determined by a combination of NOEs, NH exchange data, 3JHN alpha coupling constants, and chemical shifts of 1H alpha, 13C alpha, and 13 C beta. The protein has been found to consist of seven helices, all connected by turns or loops. Six of the seven helices (all but the C-terminal helix) form three separate helix-turn-helix motifs. The two full ANK repeats in myotrophin are characteristic of multiple turns fol...Continue Reading

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Citations

Aug 26, 1999·The Journal of Peptide Research : Official Journal of the American Peptide Society·S BhattacharjyaP Balaram
Jun 12, 2010·The Journal of Biological Chemistry·Adam ZwolakNico Tjandra
Dec 19, 2006·Journal of Molecular Biology·Diego U FerreiroElizabeth A Komives
Nov 23, 2006·Journal of Molecular Biology·Alan R Lowe, Laura S Itzhaki
Oct 12, 2000·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·H C SchröderW E Müller
Aug 10, 2006·The Journal of Biological Chemistry·Nandini BhattacharyaJohn A Cooper

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