Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure

McLachlan, Anton; Stewart, Murray

doi:10.1016/s0022-2836(75)80119-7

Cited by 691 publications

(480 citation statements)

References 33 publications

Supporting

Mentioning

450

Contrasting

Unclassified

Order By: Relevance

“…3c). As predicted from theoretical considerations [18] and confirmed in the structure of GCN4, no ionic interactions are observed between residues in e and g of the same heptad. Unlike GCN4, the f17 dinaer contains two charged residues in the hydrophobic core which are contributed by the 7 subunit (Lys l-~ in a and Glu 29 in at).…”

Section: A Model For the Fly N-terminal Do-mainsupporting

confidence: 70%

Do G protein subunits associate via a three‐stranded coiled coil?

Lupas¹,

Lupas²,

Stock³

1992

FEBS Letters

View full text Add to dashboard Cite

We used a computer-based prediction algorithm to identify probable coded.cod segments at the N-termini of G protetn t~, ]/and 7 subumts, This result indicates that (3 protein tamers may form v~a a three-stranded coded coil. Previous b~ochem~cal results had shown that ~he N-lermm~ of r, and fl are revolved m subunit interactions. Here we present a ~tructural model for the N-terminal domain of P7 and a hypothesis for the rcvcr~ible assocmtlon of ,, to PT.

show abstract

Section: A Model For the Fly N-terminal Do-mainsupporting

confidence: 70%

Do G protein subunits associate via a three‐stranded coiled coil?

Lupas¹,

Lupas²,

Stock³

1992

FEBS Letters

View full text Add to dashboard Cite

show abstract

“…Tropomyosin shows complete R-helix in CD spectroscopy (Pato et al, 1980), and its sequence displays the heptad repeats typical of coiled coils (McLachlan & Stewart, 1975). …”

Section: Desmin Rod and Other Coiled-coil Proteinsmentioning

confidence: 99%

Specific Recognition of Coiled Coils by Infrared Spectroscopy: Analysis of the Three Structural Domains of Type III Intermediate Filament Proteins

et al. 1996

View full text Add to dashboard Cite

The central domain of cytoplasmic intermediate filament (IF) proteins from vertebrates contains some 310 residues and forms a double-stranded coiled coil (rod) with a length of about 46 nm. The flanking terminal domains show a high cell type specific variability both in sequence and in length. Using Fourier transform infrared (FTIR) spectroscopy we measured secondary structures of isolated domains of type III and IV IF proteins and of the soluble tetramers and the filaments formed by type III IF proteins. The amide I spectrum of the desmin rod is virtually identical to the spectra of other coiled-coil proteins such as tropomyosin and the myosin rod. All these double-stranded coiled coils reveal spectra distinctly different from classical R-helical spectra. The spectrum of coiled coils is a triplet of approximately equally strong bands. One band occurs at normal R-helix position, while the other two are found at lower wavenumbers. Theoretical aspects of these findings are discussed in the accompanying paper by W. C. Reisdorf and S. Krimm [(1996[( ) Biochemistry 35, 1383[( -1386. The amino-terminal head domain of desmin has a multicomponent spectrum with major fractions of -sheet. The carboxy-terminal tail domains of desmin and the neurofilament proteins L and H, the latter in the phosphorylated and in the dephosphorylated forms, have very similar FTIR spectra, indicating mostly random structure. The spectrum of desmin type III protofilaments is very similar to the sum of the spectra of the three isolated domains. Polymerization into filaments seems to induce a small change in secondary structure.

show abstract

“…The sequences of coiled coils have a characteristic heptad repeat (abcdefg) n (McLachlan & Stewart, 1975). Residues at positions a and d are in general occupied by hydrophobic residues and form an interface between two or more helices (in leucine zippers, position d is occupied by Leu residues).…”

mentioning

confidence: 99%

Method for Predicting the State of Association of Discretized Protein Models. Application to Leucine Zippers^†

1996

View full text Add to dashboard Cite

A method that employs a transfer matrix treatment combined with Monte Carlo sampling has been used to calculate the configurational free energies of folded and unfolded states of lattice models of proteins. The method is successfully applied to study the monomer-dimer equilibria in various coiled coils. For the short coiled coils, GCN4 leucine zipper, and its fragments, Fos and Jun, very good agreement is found with experiment. Experimentally, some subdomains of the GCN4 leucine zipper form stable dimeric structures, suggesting the regions of differential stability in the parent structure. Our calculations suggest that the stabilities of the subdomains are in general different from the values expected simply from the stability of the corresponding fragment in the wild type molecule. Furthermore, parts of the fragments structurally rearrange in some regions with respect to their corresponding wild type positions. Our results suggest for an Asn in the dimerization interface at least a pair of hydrophobic interacting helical turns at each side is required to stabilize the stable coiled coil. Finally, the specificity of heterodimer formation in the Fos-Jun system comes from the relative instability of Fos homodimers, resulting from unfavorable intra-and interhelical interactions in the interfacial coiled coil region.

show abstract

Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure

Cited by 691 publications

References 33 publications

Do G protein subunits associate via a three‐stranded coiled coil?

Do G protein subunits associate via a three‐stranded coiled coil?

Specific Recognition of Coiled Coils by Infrared Spectroscopy: Analysis of the Three Structural Domains of Type III Intermediate Filament Proteins

Method for Predicting the State of Association of Discretized Protein Models. Application to Leucine Zippers^†

Contact Info

Product

Resources

About

Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure

Cited by 691 publications

References 33 publications

Do G protein subunits associate via a three‐stranded coiled coil?

Do G protein subunits associate via a three‐stranded coiled coil?

Specific Recognition of Coiled Coils by Infrared Spectroscopy: Analysis of the Three Structural Domains of Type III Intermediate Filament Proteins

Method for Predicting the State of Association of Discretized Protein Models. Application to Leucine Zippers†

Contact Info

Product

Resources

About

Method for Predicting the State of Association of Discretized Protein Models. Application to Leucine Zippers^†