Coiled coils: a highly versatile protein folding motif

Burkhard, Peter; Stetefeld, Jörg; Strelkov, S.V.

doi:10.1016/s0962-8924(00)01898-5

Cited by 949 publications

(825 citation statements)

References 64 publications

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“…Residue R93 is located in position a of the predicted coiled coil structure of helix α-3 (Fig 1), and as stated above this is a highly conserved amino acid within the Cry toxin family. The presence of polar residues in the apolar interface has been documented for some coiled coil structures, it is correlated with proper alignment, orientation and selectivity of coiled-coils and contribute considerably to their stability [5,9]. In addition, in has been reported that a salt bridge within the α-helix that forms the coiled-coil stabilizes this structure and is important to trigger the coiled-coil [24].…”

Section: Mutagenesis Of Helix α-3 Of Different Cry Toxinsmentioning

confidence: 95%

“…These coiled-coils constitute an important protein-folding motif formed in the interaction between two to five α-helices. They are involved in oligomerization of several proteins, forming specific oligomers with high thermodynamic stability [5,9]. The primary structure of coiled-coil structures is characterized by heptads of residues, (abcdefg) n , with a unique pattern of internal a and d positions occupied mostly by apolar residues forming an hydrophobic core and positions g and e occupied by charged residues.…”

Section: Role Of Coiled Coil Structures In Oligomerization Of Differementioning

confidence: 99%

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The pre-pore from Bacillus thuringiensis Cry1Ab toxin is necessary to induce insect death in Manduca sexta

et al. 2008

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The insecticidal Cry toxins from Bacillus thuringiensis bacteria are pore-forming toxins that lyse midgut epithelial cells in insects. We have previously proposed that they form pre-pore oligomeric intermediates before membrane insertion.For formation of these oligomers coiled-coil structures are important, and helix α-3 from Cry toxins could form coiled-coils. Our data shows that different mutations in helix α-3 are affected in pore formation and toxicity. Mutants affected in toxicity bind Bt-R 1 receptor with a similar K D as the wild type toxin but do not form oligomers nor induce pore formation in planar lipid bilayers, indicating that the pre-pore oligomer is an obligate intermediate in the intoxication of Cry1Ab toxin and that interaction of monomeric Cry1Ab with Bt-R 1 is not enough to kill susceptible larvae.

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Section: Mutagenesis Of Helix α-3 Of Different Cry Toxinsmentioning

confidence: 95%

Section: Role Of Coiled Coil Structures In Oligomerization Of Differementioning

confidence: 99%

The pre-pore from Bacillus thuringiensis Cry1Ab toxin is necessary to induce insect death in Manduca sexta

et al. 2008

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“…2,3 The individual heptad residues occupying the positions a and d are hydrophobic and permit the association of different coiled-coil strands following the knobs-into-holes model proposed by Crick in 1953. 4 The association of residues in positions a and d create a tight hydrophobic core that is stabilized by ionic interactions of polar and charged amino acids in positions e and g. 2,[5][6][7] The residues in the remaining positions are normally polar and are exposed to the solvent (Fig. 1).…”

Section: Introductionmentioning

confidence: 99%

Induced heterodimerization and purification of two target proteins by a synthetic coiled‐coil tag

Fernández-Rodríguez

Marlovits

2012

Protein Science

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A synthetic de novo designed heterodimeric coiled-coil was used to copurify two target fluorescent proteins, Venus and enhanced cyan fluorescent protein (ECFP). The coiled-coil consists of two 21-amino acid repetitive sequences, (EIAALEK) 3 and (KIAALKE) 3 , named E3 and K3, respectively. These sequences were fused to the C-termini of ECFP or Venus followed by either a strep-or a his-tag, respectively, for affinity purification. Mixed lysates of Venus-K3 and ECFP-E3 were subjected to consecutive affinity purification and showed highly specific association between the coiled-coil pair by SDS-PAGE, gel filtration, isothermal titration calorimetry (ITC), and fluorescence resonance energy transfer (FRET). The tagged proteins eluted as heterodimers at the concentrations tested. FRET analysis further showed that the coiled-coil pair was stable in buffers commonly used for protein purification, including those containing high salt concentration and detergent. This study shows that the E3/K3 pair is very well suited for the copurification of two target proteins expressed in vivo because of its high specificity: it forms exclusively heterodimers in solution, it does not interact with any cellular proteins and it is stable under different buffer conditions.

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“…The coiled coil, which is among the most frequently encountered folding motifs found in nature, is a superhelical structure that is composed of two to five ␣ helices closely wrapped around each other. 62,63 Recently, we and others have explored the coiled-coil motif to direct the self-assembly of PEGbased hybrid block copolymers. 35,36 Circular dichroism and analytical ultracentrifugation experiments have indicated that the coiled-coil sequences mediate the formation of essentially uniform nanoobjects, in which a core composed of a discrete number of ␣-helical peptides is closely encapsulated in a PEG shell.…”

Section: Self-assembly and Supramolecular Architecturesmentioning

confidence: 99%

Biological–synthetic hybrid block copolymers: Combining the best from two worlds

Klok

2004

J. Polym. Sci. A Polym. Chem.

274

142

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ABSTRACT:Although biopolymers and synthetic polymers share many common features, each of these two classes of materials is also characterized by a distinct and very specific set of advantages and disadvantages. Combining biopolymer elements with synthetic polymers into a single macromolecular conjugate is an interesting strategy for synergetically merging the properties of the individual components and overcoming some of their limitations. This article focuses on a special class of biological-synthetic hybrids that are obtained by site-selective conjugation of a protein or peptide and a synthetic polymer. The first part of the article gives an overview of the different liquid-phase and solidphase techniques that have been developed for the synthesis of well-defined, that is, site-selectively conjugated, synthetic polymer-protein hybrids. In the second part, the properties and potential applications of these materials are discussed. The conjugation of biological and synthetic macromolecules allows the modulation of protein binding and recognition properties and is a powerful strategy for mediating the self-assembly of synthetic polymers. Synthetic polymer-protein hybrids are already used as medicines and show significant promise for bioanalytical applications and bioseparations.

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Coiled coils: a highly versatile protein folding motif

Cited by 949 publications

References 64 publications

The pre-pore from Bacillus thuringiensis Cry1Ab toxin is necessary to induce insect death in Manduca sexta

The pre-pore from Bacillus thuringiensis Cry1Ab toxin is necessary to induce insect death in Manduca sexta

Induced heterodimerization and purification of two target proteins by a synthetic coiled‐coil tag

Biological–synthetic hybrid block copolymers: Combining the best from two worlds

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