Structure, three-dimensional calmodulin

Babu, Y.S., et al. Three-dimensional structure of calmodulin. Nature 315 37-40, 1985. 

This technique has been described as a general method of studying protein-protein interactions as well as a method for investigating the three-dimensional structure of individual proteins (Muller et al., 2001 Back et al., 2003 Dihazi and Sinz, 2003 Sinz, 2003 Sinz, 2006). It also has been used for the study of the interactions of cytochrome C and ribonuclease A (Pearson et al., 2002), to investigate the interaction of calmodulin with a specific peptide binder (Kalkhof et al., 2005a Schmidt et al., 2005), and for probing laminin self-interaction (Kalkhof et al., 2005b). 

Thiosulfate cyanide sulfurtransferase symmetry in 78 TTiiouridine 234 Three-dimensional structures of aconitase 689 adenylate kinase 655 aldehyde oxido-reductase 891 D-amino acid oxidase 791 a-amylase, pancreatic 607 aspartate aminotransferase 57,135 catalytic intermediates 752 aspartate carbamyltransferase 348 aspartate chemoreceptor 562 bacteriophage P22 66 cadherin 408 calmodulin 317 carbonic acid anhydrase I 679 carboxypeptidase A 64 catalase 853 cholera toxin 333, 546 chymotrypsin 611 citrate synthase 702, 703 cutinase 134 cyclosporin 488 cytochrome c 847 cytochrome c peroxidase 849 dihydrofolate reductase 807 DNA 214, 223,228,229, 241 DNA complex... 

Figure 2. Improvement of yellow cameleon by using a circularly permuted YFP variant. (A) The three-dimensional structure of GFP with the positions of the original (Metl) and new N-termini (Aspl73). (B) Domain structures of YCS.12 and YC3.60. CaM, Xenopus calmodulin Ml3, a CaM binding peptide derived from myosin light chain kinase (C, D) Emission spectra of YCS. 12 (C) and YC3.60 (D) (excitation at 435 nm) at zero (doted line) and saturated Ca (solid line). (E) A series of confocal pseudo-B/W images showing propagation of [Ca c- These images were taken at...

A ribbon backbone representation of the three-dimensional structure of turkey-skeletal-muscle troponin C according to Herzberg and James. The crystals were grown at pH 5 in the presence of excess Ca , and at this low pH only Ca ions bound to the high-affinity domain (the C-terminal domain) are observed. Note the high stmctural homology with calmodulin (Figure 3.17). 

Figure 1. Three-dimensional structures of the intracellular EF-hand calcium-binding proteins calmodulin (3cln), parvalbumin (5cpv), and calbindinD9k (4icb).

Kolodziej, S.J., Hudmon, A., Waxham, M.N. and Stoops, J.K. (2000) Three-dimensional reconstructions of calcium/calmodulin-de-pendent (CaM) kinase Ilalpha and truncated CaM kinase Ilalpha reveal a unique organization for its structural core and functional domains. J.Biol.Chem., 275, 14354-14359. 

FIGURES Amodelof the two-dimensional structure of domain 4 derived from structural and functional studies. This hypothetical structure shows domain 4 of CD bound to Ca +calmodulin. Sites A,B, and B are indicated as including both lobes of calmodulin bound in an extended conformation, together with CD tryptophans 716,749, and 779. The peptide chain is looped so that the three tryptophans and tyrosine 682 and histidine 667 are within 1.5 nm of cysteine 636. The exons are indicated by alternating shading of the peptide chain. Exon 11 is the loop at the bottom, which includes tryptophan 749 and the MAP kinase site serine 759. 

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