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

Ward Lutz, Elena M. Frank, Theodore A. Craig, Richele Thompson, Ronald A. Venters, Doug Kojetin, John Cavanagh, Rajiv Kumar

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

Calbindin D28K is an EF-hand containing protein that plays a vital role in neurological function. We now show that calcium-loaded calbindin D28K 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 D28K and Ran-binding protein M may be important in calbindin D28K function.

Original languageEnglish (US)
Pages (from-to)1186-1192
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume303
Issue number4
DOIs
StatePublished - Apr 18 2003

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Calbindin 1
Nuclear magnetic resonance spectroscopy
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
Calcium
EF Hand Motifs
Proteins
Microtubules
Peptides
Ran binding protein 9

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Calbindin D28K interacts with Ran-binding protein M : Identification of interacting domains by NMR spectroscopy. / Lutz, Ward; Frank, Elena M.; Craig, Theodore A.; Thompson, Richele; Venters, Ronald A.; Kojetin, Doug; Cavanagh, John; Kumar, Rajiv.

In: Biochemical and Biophysical Research Communications, Vol. 303, No. 4, 18.04.2003, p. 1186-1192.

Research output: Contribution to journalArticle

Lutz, Ward ; Frank, Elena M. ; Craig, Theodore A. ; Thompson, Richele ; Venters, Ronald A. ; Kojetin, Doug ; Cavanagh, John ; Kumar, Rajiv. / Calbindin D28K interacts with Ran-binding protein M : Identification of interacting domains by NMR spectroscopy. In: Biochemical and Biophysical Research Communications. 2003 ; Vol. 303, No. 4. pp. 1186-1192.
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