Modeling α-helical coiled-coil interactions: The axial and azimuthal alignment of 1B segments from vimentin intermediate filaments

2002 ◽  
Vol 50 (2) ◽  
pp. 207-212 ◽  
Author(s):  
Thomasin A. Smith ◽  
Paul D. Hempstead ◽  
Christopher C. Palliser ◽  
David A.D. Parry
Keyword(s):  
Intermediate Filaments ◽  
Coiled Coil

Plectin: A Cytolinker by Design

1999 ◽  
Vol 380 (2) ◽  
pp. 151-158 ◽  
Author(s):  
F.A. Steinböck ◽  
G. Wiche
Keyword(s):  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Transmembrane Protein ◽  
Coiled Coil ◽  
Cytoskeletal Protein ◽  
Terminal Domain ◽  
Junctional Proteins ◽  
Molecular Backbone ◽  
Cytoskeletal Elements

Abstract Plectin is a cytoskeletal protein of > 500 kDa that forms dumbbell-shaped homodimers comprising a central parallel α-helical coiled coil rod domain flanked by globular domains, thus providing a molecular backbone ideally suited to mediate the protein's interactions with an array of other cytoskeletal elements. Plectin self-associates and interacts with actin and intermediate filament cytoskeleton networks at opposite ends, and it binds at both ends to the hemidesmosomal transmembrane protein integrin beta-4, and likely to other junctional proteins. The central coiled coil rod domain can form bridges over long stretches and serves as a flexible linker between the structurally diverse N-terminal domain and the highly conserved C-terminal domain. Plectin is also a target of p34cdc2 kinase that regulates its dissociation from intermediate filaments during mitosis.

scholarly journals The primary structure of component 8c-1, a subunit protein of intermediate filaments in wool keratin. Relationships with proteins from other intermediate filaments

1986 ◽  
Vol 236 (3) ◽  
pp. 695-703 ◽  
Author(s):  
L M Dowling ◽  
W G Crewther ◽  
A S Inglis
Keyword(s):  
Amino Acid ◽  
Intermediate Filaments ◽  
Coiled Coil ◽  
Amino Acid Sequences ◽  
British Library ◽  
Type I ◽  
Intermediate Filament Proteins ◽  
Complete Sequences ◽  
Acetyl Group ◽  
Keratin Filament

Component 8c-1, one of four highly homologous component-8 subunit proteins present in the microfibrils of wool, was isolated as its S-carboxymethyl derivative and its amino acid sequence was determined. Large peptides were isolated after cleaving the protein chemically or enzymically and the sequence of each was determined with an automatic Sequenator. The peptides were ordered by sequence overlaps and, in some instances, by homology with known sequences from other component-8 subunits. The C-terminal residues were identified by three procedures. Full details of the various procedures used have been deposited as Supplementary Publication SUP 50133 (4 pp.) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1986) 233, 5. The result showed that the protein comprises 412 residues and has an Mr, including the N-terminal acetyl group, of 48,300. The sequence of residues 98-200 of component 8c-1 was found to correspond to the partial or complete sequences of four homologous type I helical segments previously isolated from helical fragments recovered from chymotryptic digests of microfibrillar proteins of wool [Crewther & Dowling (1971) Appl. Polym. Symp. 18, 1-20; Crewther, Gough, Inglis & McKern (1978) Text. Res. J. 48, 160-162; Gough, Inglis & Crewther (1978) Biochem. J. 173, 385]. Considered in relation to amino acid sequences of other intermediate-filament proteins, the sequence is in accord with the view that keratin filament proteins are of two types [Hanukoglu & Fuchs (1983) Cell (Cambridge, Mass.) 33, 915-924]. Filament proteins from non-keratinous tissues, such as desmin, vimentin, neurofilament proteins and the glial fibrillary acidic protein, which form monocomponent filaments, constitute a third type. It is suggested that as a whole the proteins from intermediate filaments be classed as filamentins, the three types at present identified forming subgroups of this class. The significant homologies between types I, II and III occur almost exclusively in segments of the chain that have been identified as having a coiled-coil structure together with the relatively short sections connecting these segments. The non-coiled-coil segments at the C- and N-termini show no significant homology between types, nor is homology in these segments apparent in all members of one type. Component 8c-1 does not show homology in its terminal segments with the known sequence of any other filamentin.(ABSTRACT TRUNCATED AT 400 WORDS)

scholarly journals CCFold: rapid and accurate prediction of coiled-coil structures and application to modelling intermediate filaments

2017 ◽  
Author(s):  
Dmytro Guzenko ◽  
Sergei V. Strelkov
Keyword(s):  
Intermediate Filaments ◽  
Coiled Coil ◽  
General Purpose ◽  
Coiled Coils ◽  
Filament Assembly ◽  
Protein Dimer ◽  
Protein Classes ◽  
Elementary Building ◽  
Experimental Structure ◽  
Or Modelling

AbstractAccurate molecular structure of the protein dimer representing the elementary building block of intermediate filaments (IFs) is essential towards the understanding of the filament assembly, rationalizing their mechanical properties and explaining the effect of disease-related IF mutations. The dimer contains a ∼300-residue long α-helical coiled coil which is not assessable to either direct experimental structure determination or modelling using standard approaches. At the same time, coiled coils are well-represented in structural databases. Here we present CCFold, a generally applicable threading-based algorithm which produces coiled-coil models from protein sequence only. The algorithm is based on a statistical analysis of experimentally determined structures and can handle any hydrophobic repeat patterns in addition to the most common heptads. We demonstrate that CCFold outperforms general-purpose computational folding in terms of accuracy, while being faster by orders of magnitude. By combining the CCFold algorithm and Rosetta folding we generate representative dimer models for all IF protein classes. The source code is freely available at https://github.com/biocryst/IF

scholarly journals Effect of shampoo, conditioner and permanent waving on the molecular structure of human hair

PeerJ ◽  
2015 ◽  
Vol 3 ◽  
pp. e1296 ◽  
Author(s):  
Yuchen Zhang ◽  
Richard J. Alsop ◽  
Asfia Soomro ◽  
Fei-Chi Yang ◽  
Maikel C. Rheinstädter
Keyword(s):  
Intermediate Filaments ◽  
Coiled Coil ◽  
Coiled Coils ◽  
X Ray Diffraction ◽  
Membrane Complex ◽  
Disulfide Linkages ◽  
Coil Structure ◽  
Single Use ◽  
Keratin Proteins ◽  
Cell Membrane Complex

The hair is a filamentous biomaterial consisting of thecuticle, thecortexand themedulla, all held together by the cell membrane complex. Thecortexmostly consists of helical keratin proteins that spiral together to form coiled-coil dimers, intermediate filaments, micro-fibrils and macro-fibrils. We used X-ray diffraction to study hair structure on the molecular level, at length scales between ∼3–90 Å, in hopes of developing a diagnostic method for diseases affecting hair structure allowing for fast and noninvasive screening. However, such an approach can only be successful if common hair treatments do not affect molecular hair structure. We found that a single use of shampoo and conditioner has no effect on packing of keratin molecules, structure of the intermediate filaments or internal lipid composition of the membrane complex. Permanent waving treatments are known to break and reform disulfide linkages in the hair. Single application of a perming product was found to deeply penetrate the hair and reduce the number of keratin coiled-coils and change the structure of the intermediate filaments. Signals related to the coiled-coil structure of theα-keratin molecules at 5 and 9.5 Å were found to be decreased while a signal associated with the organization of the intermediate filaments at 47 Å was significantly elevated in permed hair. Both these observations are related to breaking of the bonds between two coiled-coil keratin dimers.

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