Calmodulin superfamily

Ikura M, Ames JB (2006) Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily two ways to promote multifunctionality. Proc Natl Acad Sci USA 103 1159-1164... 

GCAPs belong to the EF-hand motif-containing superfamily of Ca2+-binding proteins from the calmodulin superfamily (Lewit-Bentley and Rety, 2000 Bhattacharya et al., 2004). The structures of several members of the recoverin branch of the EF-hand... 

Houdusse, A., Love, M. L., Dominguez, R., Grabarek, Z., and Cohen, C. (1997). Structures of four Ca2+-bound troponin C at 2.0 A resolution Further insights into the Ca2+-switch in the calmodulin superfamily. Structure 5, 1695-1711. 

Redesign of Ca fMg Specificity. Proteins in the calmodulin superfamily (including troponin C, parvalbumin (PV) and oncomodulin (OM)) share similar overall structure and yet have different selectivity for Ca and Mg see Calcium-binding Proteins, Cation-activated Enzymes). For example, PV and OM have four helix-tum-helix domains, two of which contain mixed Ca /Mg sites and two Ca -specific sites. The mixed Ca /Mg sites have been converted to Ca -specific sites by replacing amino acids with the corresponding residues in the Ca -specific site. " ... 

During recent years, groups interested in the role of Ca in secretion and in the control of membrane cytoskeleton have identified some intracellular phospholipid-binding proteins that appear to be distinct from the calmodulin superfamily these include lipocortin, endonexin, calelectrin, p36, and calpac-tin These membrane-binding proteins are collectively called annexins, and contain repeated domains distinct from EF-hands. The Ca sites are very similar to that observed in phospholipase A2, as shown by the recently determined x-ray structure of annexin A condensed overview of the interaction of Ca + with intracellular proteins is shown in Figure 3.16. We will now go on to discuss the molecular properties of some of the proteins mentioned above, starting with calmodulin. 

Calbindin Dg, previously known as intestinal calcium binding protein, is the smallest (75 amino acids) in the calmodulin superfamily of proteins. A special characteristic of this EF-hand protein is that the first metal binding loop is modified compared to the typical EF-hand loop, a pseudo EF-hand, a common feature for... 

Because NO synthases belong to the same superfamily of enzymes as cytochrome P-450, they are able to produce not only nitric oxide (although it is undoubtedly their main function) but also other free radicals, first of all, superoxide. In 1992, Pou et al. [148] showed that brain nitric oxide synthase (NOS I) produced superoxide identified as a DMPO—OOH adduct in a calcium- or calmodulin-dependent manner. This finding was confirmed in numerous studies for all three isoforms of NO synthase. Although the structures of all the three NO oxidase... 

Martin-Padura I, Lostaglio S, Schneemann M, LW, Romano M, Fruscella P, Panzeri C, Stoppacciaro A, Ruco L, Villa A, Simmons D, Dejana E (1998) Junctional adhesion molecule, a novel member of the immunoglobulin superfamily that distributes at intercellular junctions and modulates monocyte transmigration. J Cell Biol 142 117-127 Martinez-Estrada OM, Villa A, Breviario F, Orsenigro F, Dejana E, Bazzoni G (2001) Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial Caco-2 cells. J Biol Chem 276 9291-9296... 

Parvalbumin is an intracellular calcium-binding protein in the EF-hand superfamily of calcium-binding proteins including troponin C, calmodulin, SIOOB, and calbindin (Yanez et al, 2012). Parvalbumin is a cytosolic protein that... 

---