@article{kordys_bobay_thompson_venters_cavanagh_2007, title={Peptide binding proclivities of calcium loaded calbindin-D28k}, volume={581}, ISSN={["0014-5793"]}, DOI={10.1016/j.febslet.2007.09.004}, abstractNote={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 Ca2+‐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.}, number={24}, journal={FEBS LETTERS}, author={Kordys, David R. and Bobay, Benjamin G. and Thompson, Richele J. and Venters, Ronald A. and Cavanagh, John}, year={2007}, month={Oct}, pages={4778–4782} }
 @article{kojetin_venters_kordys_thompson_kumar_cavanagh_2006, title={Structure, binding interface and hydrophobic transitions of Ca2+-loaded calbindin-D-28K}, volume={13}, DOI={10.1038/nsmb1112d}, number={7}, journal={Nature Structural & Molecular Biology}, author={Kojetin, D. J. and Venters, R. A. and Kordys, D. R. and Thompson, R. J. and Kumar, R. and Cavanagh, J.}, year={2006}, pages={641–647} }
 @article{venters_benson_craig_paul_kordys_thompson_naylor_kumar_cavanagh_2003, title={The effects of Ca2+ binding on the conformation of calbindin D-28K: A nuclear magnetic resonance and microelectrospray mass spectrometry study}, volume={317}, ISSN={["0003-2697"]}, DOI={10.1016/S0003-2697(03)00084-8}, abstractNote={Calbindin D(28K) is a six-EF-hand calcium-binding protein found in the brain, peripheral nervous system, kidney, and intestine. There is a paucity of information on the effects of calcium binding on calbindin D(28K) structure. To further examine the mechanism and structural consequences of calcium binding to calbindin D(28K) we performed detailed complementary heteronuclear NMR and microelectrospray mass spectrometry investigations of the calcium-induced conformational changes of calbindin D(28K). The combined use of these two powerful analytical techniques clearly and very rapidly demonstrates the following: (i). apo-calbindin D(28K) has an ordered structure which changes to a notably different ordered conformation upon Ca(2+) loading, (ii). calcium binding is a sequential process and not a simultaneous event, and (iii). EF-hands 1, 3, 4, and 5 take up Ca(2+), whereas EF-hands 2 and 6 do not. Our results support the opinion that calbindin D(28K) has characteristics of both a calcium sensor and a buffer.}, number={1}, journal={ANALYTICAL BIOCHEMISTRY}, author={Venters, RA and Benson, LM and Craig, TA and Paul, KH and Kordys, DR and Thompson, R and Naylor, S and Kumar, R and Cavanagh, J}, year={2003}, month={Jun}, pages={59–66} }