Nuclear magnetic resonance assignments and secondary structure of bovine S100β protein

Peter M. Kilby; Linda J. Van Eldik; Gordon C.K. Roberts

doi:10.1016/0014-5793(95)00296-L

Nuclear magnetic resonance assignments and secondary structure of bovine S100β protein

Peter M. Kilby, Linda J. Van Eldik, Gordon C.K. Roberts

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

S100β is a neurite extension factor and has been implicated in Alzheimer's disease and Down's syndrome. It belongs to a group of low molecular weight calcium-binding proteins containing the helix-loop-helix calcium binding motif. The structure of only one S100 protein, calbindin D_9k, which has the lowest sequence similarity to the other members of the S100 group has been determined. We report the NMR assignments and secondary structure of calcium-free S100β. The secondary structure is similar to that of calbindin D_9k, determined using NMR, except that there is clear evidence for an additional well ordered 5-residue α-helix in S100β.

Original language	English
Pages (from-to)	90-96
Number of pages	7
Journal	FEBS Letters
Volume	363
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(95)00296-L
State	Published - Apr 17 1995

Bibliographical note

Funding Information:
Acknowledgements: This work was supported by a Wellcome Trust Research Fellowship to P.M.K. and by National Institutes of Health Grant AG10208 to L.V.E.

Keywords

Calcium-binding protein
Nuclear magnetic resonance
S-100
S100
Secondary structure

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(95)00296-L

Cite this

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title = "Nuclear magnetic resonance assignments and secondary structure of bovine S100β protein",

abstract = "S100β is a neurite extension factor and has been implicated in Alzheimer's disease and Down's syndrome. It belongs to a group of low molecular weight calcium-binding proteins containing the helix-loop-helix calcium binding motif. The structure of only one S100 protein, calbindin D9k, which has the lowest sequence similarity to the other members of the S100 group has been determined. We report the NMR assignments and secondary structure of calcium-free S100β. The secondary structure is similar to that of calbindin D9k, determined using NMR, except that there is clear evidence for an additional well ordered 5-residue α-helix in S100β.",

keywords = "Calcium-binding protein, Nuclear magnetic resonance, S-100, S100, Secondary structure",

author = "Kilby, {Peter M.} and {Van Eldik}, {Linda J.} and Roberts, {Gordon C.K.}",

note = "Funding Information: Acknowledgements: This work was supported by a Wellcome Trust Research Fellowship to P.M.K. and by National Institutes of Health Grant AG10208 to L.V.E.",

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AU - Kilby, Peter M.

AU - Van Eldik, Linda J.

AU - Roberts, Gordon C.K.

N1 - Funding Information: Acknowledgements: This work was supported by a Wellcome Trust Research Fellowship to P.M.K. and by National Institutes of Health Grant AG10208 to L.V.E.

PY - 1995/4/17

Y1 - 1995/4/17

N2 - S100β is a neurite extension factor and has been implicated in Alzheimer's disease and Down's syndrome. It belongs to a group of low molecular weight calcium-binding proteins containing the helix-loop-helix calcium binding motif. The structure of only one S100 protein, calbindin D9k, which has the lowest sequence similarity to the other members of the S100 group has been determined. We report the NMR assignments and secondary structure of calcium-free S100β. The secondary structure is similar to that of calbindin D9k, determined using NMR, except that there is clear evidence for an additional well ordered 5-residue α-helix in S100β.

AB - S100β is a neurite extension factor and has been implicated in Alzheimer's disease and Down's syndrome. It belongs to a group of low molecular weight calcium-binding proteins containing the helix-loop-helix calcium binding motif. The structure of only one S100 protein, calbindin D9k, which has the lowest sequence similarity to the other members of the S100 group has been determined. We report the NMR assignments and secondary structure of calcium-free S100β. The secondary structure is similar to that of calbindin D9k, determined using NMR, except that there is clear evidence for an additional well ordered 5-residue α-helix in S100β.

KW - Calcium-binding protein

KW - Nuclear magnetic resonance

KW - S-100

KW - S100

KW - Secondary structure

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Nuclear magnetic resonance assignments and secondary structure of bovine S100β protein

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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