Skip to main content
Journal cover image

Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy.

Publication ,  Journal Article
Lutz, W; Frank, EM; Craig, TA; Thompson, R; Venters, RA; Kojetin, D; Cavanagh, J; Kumar, R
Published in: Biochem Biophys Res Commun
April 18, 2003

Calbindin D(28K) is an EF-hand containing protein that plays a vital role in neurological function. We now show that calcium-loaded calbindin D(28K) interacts with Ran-binding protein M, a protein known to play a role in microtubule function. Using NMR methods, we show that a peptide, LASIKNR, derived from Ran-binding protein M, interacts with several regions of the calcium-loaded protein including the amino terminus and two other regions that exhibit conformational exchange on the NMR timescale. We suggest that the interaction between calbindin D(28K) and Ran-binding protein M may be important in calbindin D(28K) function.

Duke Scholars

Altmetric Attention Stats
Dimensions Citation Stats

Published In

Biochem Biophys Res Commun

DOI

ISSN

0006-291X

Publication Date

April 18, 2003

Volume

303

Issue

4

Start / End Page

1186 / 1192

Location

United States

Related Subject Headings

  • ran GTP-Binding Protein
  • S100 Calcium Binding Protein G
  • Protein Structure, Tertiary
  • Precipitin Tests
  • Nuclear Proteins
  • Molecular Sequence Data
  • Magnetic Resonance Spectroscopy
  • Cytoskeletal Proteins
  • Calbindins
  • Biochemistry & Molecular Biology
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Lutz, W., Frank, E. M., Craig, T. A., Thompson, R., Venters, R. A., Kojetin, D., … Kumar, R. (2003). Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy. Biochem Biophys Res Commun, 303(4), 1186–1192. https://doi.org/10.1016/s0006-291x(03)00499-6
Lutz, Ward, Elena M. Frank, Theodore A. Craig, Richele Thompson, Ronald A. Venters, Doug Kojetin, John Cavanagh, and Rajiv Kumar. “Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy.Biochem Biophys Res Commun 303, no. 4 (April 18, 2003): 1186–92. https://doi.org/10.1016/s0006-291x(03)00499-6.
Lutz W, Frank EM, Craig TA, Thompson R, Venters RA, Kojetin D, et al. Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy. Biochem Biophys Res Commun. 2003 Apr 18;303(4):1186–92.
Lutz, Ward, et al. “Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy.Biochem Biophys Res Commun, vol. 303, no. 4, Apr. 2003, pp. 1186–92. Pubmed, doi:10.1016/s0006-291x(03)00499-6.
Lutz W, Frank EM, Craig TA, Thompson R, Venters RA, Kojetin D, Cavanagh J, Kumar R. Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy. Biochem Biophys Res Commun. 2003 Apr 18;303(4):1186–1192.
Journal cover image

Published In

Biochem Biophys Res Commun

DOI

ISSN

0006-291X

Publication Date

April 18, 2003

Volume

303

Issue

4

Start / End Page

1186 / 1192

Location

United States

Related Subject Headings

  • ran GTP-Binding Protein
  • S100 Calcium Binding Protein G
  • Protein Structure, Tertiary
  • Precipitin Tests
  • Nuclear Proteins
  • Molecular Sequence Data
  • Magnetic Resonance Spectroscopy
  • Cytoskeletal Proteins
  • Calbindins
  • Biochemistry & Molecular Biology