Coiled coil domain

Amino acid substitutions on the native y52 8sKIpeptide, coiled-coil domain of human fibrin were able to stabilize the coiled-coil formation. These substitutions were targeted to the positions that compose the interface between coiled-coil strands while the solvent-exposed residues were left unperturbed. This strategy aimed at reducing the likelihood of immunogenicity for future in vivo apphcafion of these materials. In contrast to PEG block copolymers with end blocks that are not used for directed assembly, PEG copolymers with coiled-coil protein motives aim to enhance intermolecular interactions and control over the assembly conditions [85, 173]. 

Shen W (2005) Structure, dynamics, and properties of artificial protein hydrogels assembled through coiled-coil domains. California Institute of Technology, Pasadena... 

The coiled-coil domain frequently mediates hetero- or homodimerization. About two-thirds of a large number of TRIM proteins tested dimerize [125]. As a number of other RING finger proteins either homo- or hererodimerize, dimerization may facilitate optimal E3 activity of TRIMs. While most proteins that carry the TRIM... 

Brickley K, Smith MJ, Beck M, Stephenson FA. 2005. GRIF-1 and OIP106, members of a novel gene family of coiled-coil domain proteins association in vivo and in vitro with kinesin. J Biol Chem 280 14723-14732. 

A recurring feature of all bacteria possessing genuine 20S proteasomes is the existence of a gene, ARC, encoding a more distant member of the AAA family of ATPases, which is found upstream of the proteasome operons (Nagy et al. 1998 De Mot et al. 1999). The recombinant ARC ATPase from Rhodococcus erythropolis is a complex of two six-membered rings with ATPase activity like other proteasomal ATPases it has an N-terminal coiled-coil domain (Wolf et al. 1998). 

Dunlap It is at least a dimer. The coiled coil domain that is responsible for dimerization is essential for carrying out its function. 

J.M. Mason, K.M. Arndt, Coiled coil domains Stability, specificity, and biological implications, ChemBioChem 5(2) (2004) 170-176. 

Fig. 6 Proteins with GPR motifs. (RBD Ras binding domain, PTB phosphotyrosine binding domain, RGS regulator of G-protein signaling domain, PDZ PSD95/DLG/ZO-1 domain, cc coiled-coil domain). This figure is adapted from the thesis of Dr. Yuri Peterson...

Steimle, P.A. Licate, L. Cote, G.P. Egelhoff, T.T. Lamellipodial localization of Dictyostelium myosin heavy chain kinase A is mediated via F-actin binding by the coiled-coil domain. FEBS Lett., 516, 58-62 (2002)... 

FIGURE 24-34 Structure of SMC proteins, (a) The five domains of the SMC primary structure. N and C denoted the amino-terminal and carboxyl-terminal domains, respectively, (b) Each polypeptide is folded so that the two coiled-coil domains wrap around each other and the N and C domains come together to form a complete ATP-binding site. Two of these domains are linked at the hinge region to form the dimeric V-shaped molecule, (c) Electron micrograph of SMC proteins from Bacillus subtilis. 

The first high-resolution X-ray structure of a two-stranded a-helical coiled coil was reported by O Shea et al.127 and represented the dimerization domain of the DNA-binding protein GCN4. Since then, over 20 other proteins containing coiled-coil domains have been solved to high resolution.12 1 The X-ray crystallographic data indicate that the side chains of residues at positions a and d are almost totally buried in the dimer. 

Alfadhli, A., Steel, E., Finlay, L., Bachinger, H. P., and Barklis, E. (2002). Hantavirus nucleocapsid protein coiled-coil domains./. Biol. Chem. 277, 27103-27108. 

Beck, K., Dixon, T. W., Engel, J., and Parry, D. A. D. (1993). Ionic interactions in the coiled-coil domain of laminin determine the specificity of chain assembly. J. Mol. Biol. 231, 311-323. 

Beck, K., Gambee, J. E., Kamawal, A., and Bachinger, H. P. (1997). A single amino acid can switch the oligomerization state of the a-helical coiled-coil domain of cartilage matrix protein. EMBOJ. 16, 3767-3777. 

Delorenzi, M., and Speed, T. (2002). An HMM model for coiled-coil domains and a comparison with PSSM-based predictions. Bioinformatics 18, 617-625. 

Tarbouriech, N., Curran, J., Ruigrok, R. W. H., and Burmeister, W. P. (2000). Tetra-meric coiled coil domain of Sendai virus phosphoprotein. Nat. Struct. Biol. 7, 777-781. 

Fig. 1. Schematic diagram of (a) an intermediate filament heterodimer with coiled-coil domains 1A, IB, 2A, and 2B, and noncoiled-coil connecting linkers LI, L12, and L2. A stutter occurs in the heptad substructure at a point close to the center of segment 2B. The N-terminal globular domains (green for Type I and brown for Type II chains) are termed the heads, and the C-terminal domains (red for Type I and orange for Type II chains) are designated the tails. In (b), the heads are shown folded back over the rod domain, where it is believed that this will stabilize segment 1A. In (c), the heads are shown away from the body of the rod domain and in a position where they can interact more easily with other cellular entities. As a consequence, segment 1A may become destabilized and hence unwind to form two separate a-helical strands.

Day, C. L., and Alber, T. (2000). Crystal structure of the amino-terminal coiled-coil domain of the APC tumor suppressor. / Mol. Biol. 301, 147-156. 

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