Peptide binding proclivities of calcium loaded calbindin-D28k.
Calbindin-D28k is known to function as a calcium-buffering protein in the cell. Moreover, recent evidence shows that it also plays a role as a sensor. Using circular dichroism and NMR, we show that calbindin-D28k undergoes significant conformational changes upon binding calcium, whereas only minor changes occur when binding target peptides in its Ca(2+)-loaded state. NMR experiments also identify residues that undergo chemical shift changes as a result of peptide binding. The subsequent use of computational protein-protein docking protocols produce a model describing the interaction interface between calbindin-D28k and its target peptides.
Kordys
David R
DR
Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC 27695, USA.
Bobay
Benjamin G
BG
Thompson
Richele J
RJ
Venters
Ronald A
RA
Cavanagh
John
J
D000818:Animals; D064092:Calbindin 1; D064026:Calbindins; D002118:Calcium / Q000378:metabolism*; D002942:Circular Dichroism; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D051381:Rats; D064030:S100 Calcium Binding Protein G / Q000378:metabolism*; D017186:Titrimetry
C576500:Calb1 protein, rat; D064092:Calbindin 1; D064026:Calbindins; D010455:Peptides; D064030:S100 Calcium Binding Protein G; D002118:Calcium