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

Producción científica: Article › revisión exhaustiva

15 Citas (Scopus)

Resumen

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.

Idioma original	English
Páginas (desde-hasta)	90-96
Número de páginas	7
Publicación	FEBS Letters
Volumen	363
N.º	1-2
DOI	https://doi.org/10.1016/0014-5793(95)00296-L
Estado	Published - abr 17 1995

Nota bibliográfica

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.

Financiación

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.

Financiadores	Número del financiador
National Institutes of Health (NIH)
National Institute on Aging	P01AG010208
Wellcome Trust

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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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.",

year = "1995",

month = apr,

day = "17",

doi = "10.1016/0014-5793(95)00296-L",

language = "English",

volume = "363",

pages = "90--96",

number = "1-2",

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TY - JOUR

T1 - Nuclear magnetic resonance assignments and secondary structure of bovine S100β protein

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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UR - https://www.scopus.com/pages/publications/0028951155#tab=citedBy

U2 - 10.1016/0014-5793(95)00296-L

DO - 10.1016/0014-5793(95)00296-L

M3 - Article

C2 - 7729560

AN - SCOPUS:0028951155

SN - 0014-5793

VL - 363

SP - 90

EP - 96

JO - FEBS Letters

JF - FEBS Letters

IS - 1-2

ER -

Nuclear magnetic resonance assignments and secondary structure of bovine S100β protein

Resumen

Nota bibliográfica

Financiación

ASJC Scopus subject areas

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