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1H, 13C and 15N NMR assignments and solution secondary structure of rat Apo-S100β

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Summary

The 1H, 13C and 15N NMR assignments of the backbone and side-chain resonances of rat S100β were made at pH 6.5 and 37°C using heteronuclear multidimensional NMR spectroscopy. Analysis of the NOE correlations, together with amide exchange rate and 1Hα, 13Cα and 13Cβ chemical shift data, provided extensive secondary structural information. Thus, the secondary structure of S100β was determined to comprise four helices (Leu3-Ser18, helix I; Lys29-Leu40, helix II; Gln50-Glu62, helix III; and Phe70-Ala83, helix IV), four loops (Gly19-His25, loop I; Ser41-Glu49, loop II; Asp63-Gly66, loop III; and Cys84-Glu91, loop IV) and two β-strands (Lys26-Lys28, β-strand I and Glu67-Asp69, β-strand II). The β-strands were found to align in an antiparallel manner to form a very small β-sheet. This secondary structure is consistent with predictions that S100β contains two ‘helix-loop-helix’ Ca2+-binding motifs known as EF-hands. The alignment of the β-sheet, which brings the two EF-hand domains of S100β into close proximity, is similar to that of several other Ca2+ ion-binding proteins.

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Author notes

  1. Sanjiv Shah

    Present address: Laboratory of Biochemical Genetics, NHLBI, National Institutes of Health, Building 36, Room 4C12, 9000 Rockville Pike, 20892, Bethesda, MD, U.S.A.

  2. Dana C. Hilt

    Present address: AMGEN Inc., 1840 DeHavilland Drive, 91320-1789, Thousand Oaks, CA, U.S.A.

Authors and Affiliations

  1. Department of Biological Chemistry, University of Maryland School of Medicine, 108 North Greene Street, 21201, Baltimore, MD, U.S.A.

    Judith C. Amburgey & David J. Weber

  2. Department of Neurology, University of Maryland School of Medicine, 108 North Greene Street, 21201, Baltimore, MD, U.S.A.

    Sanjiv Shah & Dana C. Hilt

  3. National Magnetic Resonance Facility at Madison, University of Wisconsin at Madison, 420 Henry Mall, 53706-1569, Madison, WI, U.S.A.

    Frits Abildgaard

  4. Howard Hughes Medical Institute, University of Maryland Baltimore County, 21228, Baltimore, MD, U.S.A.

    Mary R. Starich

  5. Department of Chemistry and Biochemistry, University of Maryland Baltimore County, 21228, Baltimore, MD, U.S.A.

    Mary R. Starich

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  1. Judith C. Amburgey
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Amburgey, J.C., Abildgaard, F., Starich, M.R. et al. 1H, 13C and 15N NMR assignments and solution secondary structure of rat Apo-S100β. J Biomol NMR 6, 171–179 (1995). https://doi.org/10.1007/BF00211781

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