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

doi:10.1016/S0006-291X(03)00499-6

Calbindin D_28K 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

Nephrology and Hypertension

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Abstract

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.

Original language	English (US)
Pages (from-to)	1186-1192
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	303
Issue number	4
DOIs	https://doi.org/10.1016/S0006-291X(03)00499-6
State	Published - Apr 18 2003

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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

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.",

author = "Ward Lutz and Frank, {Elena M.} and Craig, {Theodore A.} and Richele Thompson and Venters, {Ronald A.} and Doug Kojetin and John Cavanagh and Rajiv Kumar",

note = "Funding Information: This work was supported by NIH Grants DK 58546, DK 25409, and DK 59505 to R.K. ",

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TY - JOUR

T1 - Calbindin D28K interacts with Ran-binding protein M

T2 - Identification of interacting domains by NMR spectroscopy

AU - Lutz, Ward

AU - Frank, Elena M.

AU - Craig, Theodore A.

AU - Thompson, Richele

AU - Venters, Ronald A.

AU - Kojetin, Doug

AU - Cavanagh, John

AU - Kumar, Rajiv

N1 - Funding Information: This work was supported by NIH Grants DK 58546, DK 25409, and DK 59505 to R.K.

PY - 2003/4/18

Y1 - 2003/4/18

N2 - 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.

AB - 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.

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Calbindin D_28K interacts with Ran-binding protein M: Identification of interacting domains by NMR spectroscopy

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