Scholars@Duke publication: The effects of Ca(2+) binding on the conformation of calbindin D(28K): a nuclear magnetic resonance and microelectrospray mass spectrometry study.

The effects of Ca(2+) binding on the conformation of calbindin D(28K): a nuclear magnetic resonance and microelectrospray mass spectrometry study.

Publication , Journal Article

Venters, RA; Benson, LM; Craig, TA; Bagu, J; Paul, KH; Kordys, DR; Thompson, R; Naylor, S; Kumar, R; Cavanagh, J

Published in: Anal Biochem

June 1, 2003

Calbindin D(28K) is a six-EF-hand calcium-binding protein found in the brain, peripheral nervous system, kidney, and intestine. There is a paucity of information on the effects of calcium binding on calbindin D(28K) structure. To further examine the mechanism and structural consequences of calcium binding to calbindin D(28K) we performed detailed complementary heteronuclear NMR and microelectrospray mass spectrometry investigations of the calcium-induced conformational changes of calbindin D(28K). The combined use of these two powerful analytical techniques clearly and very rapidly demonstrates the following: (i). apo-calbindin D(28K) has an ordered structure which changes to a notably different ordered conformation upon Ca(2+) loading, (ii). calcium binding is a sequential process and not a simultaneous event, and (iii). EF-hands 1, 3, 4, and 5 take up Ca(2+), whereas EF-hands 2 and 6 do not. Our results support the opinion that calbindin D(28K) has characteristics of both a calcium sensor and a buffer.

Duke Scholars

Author Ronald Venters Radiology

Published In

Anal Biochem

DOI

10.1016/s0003-2697(03)00084-8

ISSN

0003-2697

Publication Date

June 1, 2003

Volume

317

Issue

Start / End Page

59 / 66

Location

United States

Related Subject Headings

Spectrometry, Mass, Electrospray Ionization
S100 Calcium Binding Protein G
Recombinant Fusion Proteins
Protein Binding
Nuclear Magnetic Resonance, Biomolecular
Nitrogen Isotopes
Molecular Weight
Escherichia coli Proteins
EF Hand Motifs
Calcium

Citation

APA

Chicago

ICMJE

MLA

NLM

Venters, R. A., Benson, L. M., Craig, T. A., Bagu, J., Paul, K. H., Kordys, D. R., … Cavanagh, J. (2003). The effects of Ca(2+) binding on the conformation of calbindin D(28K): a nuclear magnetic resonance and microelectrospray mass spectrometry study. Anal Biochem, 317(1), 59–66. https://doi.org/10.1016/s0003-2697(03)00084-8

Venters, Ronald A., Linda M. Benson, Theodore A. Craig, John Bagu, Keriann H. Paul, David R. Kordys, Richele Thompson, Stephen Naylor, Rajiv Kumar, and John Cavanagh. “The effects of Ca(2+) binding on the conformation of calbindin D(28K): a nuclear magnetic resonance and microelectrospray mass spectrometry study.” Anal Biochem 317, no. 1 (June 1, 2003): 59–66. https://doi.org/10.1016/s0003-2697(03)00084-8.

Venters RA, Benson LM, Craig TA, Bagu J, Paul KH, Kordys DR, et al. The effects of Ca(2+) binding on the conformation of calbindin D(28K): a nuclear magnetic resonance and microelectrospray mass spectrometry study. Anal Biochem. 2003 Jun 1;317(1):59–66.

Venters, Ronald A., et al. “The effects of Ca(2+) binding on the conformation of calbindin D(28K): a nuclear magnetic resonance and microelectrospray mass spectrometry study.” Anal Biochem, vol. 317, no. 1, June 2003, pp. 59–66. Pubmed, doi:10.1016/s0003-2697(03)00084-8.

Venters RA, Benson LM, Craig TA, Bagu J, Paul KH, Kordys DR, Thompson R, Naylor S, Kumar R, Cavanagh J. The effects of Ca(2+) binding on the conformation of calbindin D(28K): a nuclear magnetic resonance and microelectrospray mass spectrometry study. Anal Biochem. 2003 Jun 1;317(1):59–66.