Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy.
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.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Binding Sites, Calcium-Binding Protein, Vitamin D-Dependent, Cytoskeletal Proteins, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Nuclear Proteins, Precipitin Tests, Protein Structure, Tertiary, ran GTP-Binding Protein
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Binding Sites, Calcium-Binding Protein, Vitamin D-Dependent, Cytoskeletal Proteins, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Nuclear Proteins, Precipitin Tests, Protein Structure, Tertiary, ran GTP-Binding Protein
Biochem. Biophys. Res. Commun.
Date: Apr. 18, 2003
PubMed ID: 12684061
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