Erratum to “The effects of Ca2+ binding on the conformation of calbindin D28K: A nuclear magnetic resonance and microelectrospray mass spectrometry study” [Anal. Biochem. 317 (2003) 59–66]

Calbindin D28k targets myo -inositol monophosphatase in spines and dendrites of cerebellar Purkinje neurons

“…In recent years, evidence showing that CB may be more than a simple Ca 2ϩ buffer has been accumulated by Berggård, Linse, and coworkers (7)(8)(9) and Kumar, Cavanagh, and coworkers (10,11). Their in vitro studies indicated that CB undergoes conformational changes upon Ca 2ϩ binding (8)(9)(10) and that CB interacts with myo-inositol monophosphatase (IMPase; ref.…”

“…Their in vitro studies indicated that CB undergoes conformational changes upon Ca 2ϩ binding (8)(9)(10) and that CB interacts with myo-inositol monophosphatase (IMPase; ref. 7) and Ran-binding protein M (11).…”

The X-ray structure of human calbindin-D28K: an improved model

“…There are differences in the calcium-binding residues between the individual calciumbinding loops; despite these differences in primary structure, macroscopic studies have indicated that calbindin-D28K binds calcium in a nonsequential, parallel manner (Berggå rd, Miron et al, 2002). However, other spectroscopic studies have indicated the opposite, that calcium binding is not simultaneous (Venters et al, 2003), and the differences in the calciumbinding mechanisms observed in the crystal structure support this. EF3 is the only calcium-binding loop that does not use water in the pentagonal bipyramidal coordination of the calcium ion; Glu119 at position 9 instead fulfils this role.…”

“…As in most calciumbinding proteins, the calcium ion is coordinated in the loop region between the two helices of the EF-hand; in calbindin-D28K a calcium ion is coordinated in four of the six EF-hand motifs. EF-hands 1, 3, 4 and 5 bind calcium with high affinity (Å kerfeldt et al, 1996;Venters et al, 2003). It has been shown that calbindin-D28K undergoes structural changes upon calcium binding indicative of a calcium-sensing protein (Berggå rd, Miron et al, 2002).…”

Crystallization and preliminary crystallographic analysis of human Ca2+-loaded calbindin-D28k

“…Although calbindin carries out very important physiological functions, knowledge of its overall structure remained limited until the recent NMR solution structure of Ca 2+ -loaded calbindin from Rattus norvegicus (PDB code 2g9b; Kojetin et al, 2006;Linse et al, 1997). Previous research has mainly focused on the general conformational effects of H + concentration (Berggard et al, 2000), Ca 2+ binding (Berggard et al, 2000;Venters et al, 2003;Venyaminov et al, 2004), deamidation (Vanbelle et al, 2005), disulfide-bond formation (Cedervall et al, 2005), S-nitrosation (Tao et al, 2002;Tao & English, 2003) and the binding of peptides derived from the protein targets RanBPM and IMPase3 with the aid of NMR and CD (Kordys et al, 2007).…”