Coiled coil
A coiled coil is a
Discovery
The possibility of coiled coils for α-keratin was initially somewhat controversial. Linus Pauling and Francis Crick independently came to the conclusion that this was possible at about the same time. In the summer of 1952, Pauling visited the laboratory in England where Crick worked. Pauling and Crick met and spoke about various topics; at one point, Crick asked whether Pauling had considered "coiled coils" (Crick came up with the term), to which Pauling said he had. Upon returning to the United States, Pauling resumed research on the topic. He concluded that coiled coils exist, and submitted a lengthy manuscript to the journal Nature in October. Pauling's son Peter Pauling worked at the same lab as Crick, and mentioned the report to him. Crick believed that Pauling had stolen his idea, and submitted a shorter note to Nature a few days after Pauling's manuscript arrived. Eventually, after some controversy and frequent correspondences, Crick's lab declared that the idea had been reached independently by both researchers, and that no intellectual theft had occurred.[4] In his note (which was published first due to its shorter length), Crick proposed the Coiled Coil and as well as mathematical methods for determining their structure.[5] Remarkably, this was soon after the structure of the alpha helix was suggested in 1951 by Linus Pauling and coworkers.[6] These studies were published in the absence of knowledge of a keratin sequence. The first keratin sequences were determined by Hanukoglu and Fuchs in 1982.[7][8]
Based on sequence and secondary structure prediction analyses identified the coiled-coil domains of keratins.[8] These models have been confirmed by structural analyses of coiled-coil domains of keratins.[9]
Molecular structure
Coiled coils usually contain a repeated pattern, hxxhcxc, of hydrophobic (h) and charged (c)
The
Biological roles
As coiled-coil domains are common among a significant amount of proteins in a wide variety of protein families, they help proteins fulfill various functions in the cell. Their primary feature is to facilitate protein-protein interaction and keep proteins or domains interlocked. This feature corresponds to several subfunctions, including membrane fusion, molecular spacing, oligomerization tags, vesicle movement, aid in movement proteins, cell structure, and more.[12]
Membrane Fusion
A coiled coil domain plays a role in HIV infection. Viral entry into CD4-positive cells commences when three subunits of a glycoprotein 120 (
The proteins SNAP-25, synaptobrevin, and syntaxin-1 have alpha-helices which interact with each other to form a coiled-coil SNARE complex. Zippering the domains together provides the necessary energy for vesicle fusion to occur.[17]
Molecular spacers
The coiled-coil motif may also act as a spacer between two objects within a cell. The lengths of these molecular spacer coiled-coil domains are highly conserved. The purpose of these molecular spacers may be to separate protein domains, thus keeping them from interacting, or to separate vesicles within the cell to mediate vesicle transport. An example of this first purpose is Omp‐α found in
As oligomerization tags
Because of their specific interaction coiled coils can be used as "tags" to stabilize or enforce a specific oligomerization state.
Design
The general problem of deciding on the folded structure of a protein when given the amino acid sequence (the so-called
It was recently demonstrated by Peacock, Pikramenou and co-workers that coiled coils may be self-assembled using lanthanide(III) ions as a template, thus producing novel imaging agents.[33]
Biomedical Applications
Coiled-coil motifs have been experimented on as possible building block for nanostructures, in part because of their simple design and wide range of function based primarily on facilitating protein-protein interaction. Simple guidelines for de novo synthesis of new proteins containing coiled-coil domains have led to many applications being hypothesized, including drug delivery, regenerating tissue, protein origami, and much more.[34] In regards to drug delivery, coiled-coil domains would help overcome some of the hazards of chemotherapeutic drugs, by keeping them from leaking into healthy tissue as they are transported to their target. Coiled-coil domains can be made to bind to specific proteins or cell surface markers, allowing for more precise targeting in drug delivery.[35] Other functions would be to help store and transport drugs within the body that would otherwise degrade rapidly, by creating nanotubes and other structure svia the interlocking of coiled-coil motifs.[34] By utilizing the function of oligomerization of proteins via coiled-coil domains, antigen display can be amplified in vaccines, increasing their effectiveness.[36]
The oligomerization of coiled-coil motifs allows for the creation of protein origami and protein building blocks. Metal-ligand interactions, covalent bonds, and ionic interactions have been studied to manipulate possible coiled-coil interactions in this field of study.[34] Several different nanostructures can be made by combining coiled-coil motifs such that they are self-assembling building blocks. However, several difficulties remain with stability.[37] Using peptides with coiled-coil motifs for scaffolding has made it easier to create 3D structures for cell culturing. 3D hydrogels can be made with these peptides, and then cells may be loaded into the matrix.[38] This has applications in the study of tissue, tissue engineering, and more.[34]
References
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- ^ Hager T. "Narrative 43, Coils Upon Coils". Linus Pauling and the Structure of Proteins. Oregon State University Special Collections and Archives Research Center. Retrieved May 15, 2013.
- ^ a b
Crick FH (November 1952). "Is alpha-keratin a coiled coil?". Nature. 170 (4334): 882–883. S2CID 4147931.
- ^
Pauling L, Corey RB, Branson HR (April 1951). "The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain". Proceedings of the National Academy of Sciences of the United States of America. 37 (4): 205–211. PMID 14816373.
- S2CID 35796315.
- ^ S2CID 21490380.
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- ^
Mason JM, Arndt KM (February 2004). "Coiled coil domains: stability, specificity, and biological implications". ChemBioChem. 5 (2): 170–176. S2CID 39252601.
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- ^ PMID 29400389.
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Bromley EH, Channon K, Moutevelis E, Woolfson DN (January 2008). "Peptide and protein building blocks for synthetic biology: from programming biomolecules to self-organized biomolecular systems". ACS Chemical Biology. 3 (1): 38–50. PMID 18205291.
- ^
Mahrenholz CC, Abfalter IG, Bodenhofer U, Volkmer R, Hochreiter S (May 2011). "Complex networks govern coiled-coil oligomerization--predicting and profiling by means of a machine learning approach". Molecular & Cellular Proteomics. 10 (5): M110.004994. PMID 21311038.
- ^
Harbury PB, Zhang T, Kim PS, Alber T (November 1993). "A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants". Science. 262 (5138): 1401–1407. S2CID 45833675.
- ^
Harbury PB, Kim PS, Alber T (September 1994). "Crystal structure of an isoleucine-zipper trimer". Nature. 371 (6492): 80–83. S2CID 4319206.
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Woolfson DN (2005). "The design of coiled-coil structures and assemblies". Fibrous Proteins: Coiled-Coils, Collagen and Elastomers. Advances in Protein Chemistry. Vol. 70. pp. 79–112. PMID 15837514.
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- ^ S2CID 252514360.
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Further reading
- Crick FH (1953). "The Packing of α-Helices: Simple Coiled-Coils". Acta Crystallogr. 6 (8): 689–697. .
- Nishikawa K, Scheraga HA (1976). "Geometrical criteria for formation of coiled-coil structures of polypeptide chains". Macromolecules. 9 (3): 395–407. PMID 940353.
- Harbury PB, Zhang T, Kim PS, Alber T (November 1993). "A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants". Science. 262 (5138): 1401–1407. S2CID 45833675.
- Gonzalez L, Plecs JJ, Alber T (June 1996). "An engineered allosteric switch in leucine-zipper oligomerization". Nature Structural Biology. 3 (6): 510–515. S2CID 30381026.
- Harbury PB, Plecs JJ, Tidor B, Alber T, Kim PS (November 1998). "High-resolution protein design with backbone freedom". Science. 282 (5393): 1462–1467. PMID 9822371.
- Yu YB (October 2002). "Coiled-coils: stability, specificity, and drug delivery potential". Advanced Drug Delivery Reviews. 54 (8): 1113–1129. PMID 12384310.
- Burkhard P, Ivaninskii S, Lustig A (May 2002). "Improving coiled-coil stability by optimizing ionic interactions". Journal of Molecular Biology. 318 (3): 901–910. PMID 12054832.
- Gillingham AK, Munro S (August 2003). "Long coiled-coil proteins and membrane traffic". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1641 (2–3): 71–85. PMID 12914949.
- Mason JM, Arndt KM (February 2004). "Coiled coil domains: stability, specificity, and biological implications". ChemBioChem. 5 (2): 170–176. S2CID 39252601.
External links
Prediction, detection, and visualization
- Spiricoil predict Coiled Coil and Oligormeric state from a protein sequences at archive.today (archived 2012-12-23)
- NCOILS at archive.today (archived 2002-01-11)
- Paircoil2 / Paircoil
- bCIPA Estimates Tm values for coiled coil pairs
- bCIPA library screen Screens a library of sequences against a single defined target and estimates Tm values for all coiled coils pairs.
- bCIPA Interactome Screen Screens all interactions between a selection of defined sequences and estimates Tm values for all coiled coil pairs.
- STRAP contains an algorithm to predict coiled-coils from AA-sequences.
- PrOCoil predicts the oligomerization of coiled coil proteins and visualizes the contribution of each individual amino acid to the overall oligomeric tendency.
- DrawCoil creates helical wheel diagrams for coiled coils of any oligomerization state and orientation.
Databases
- Spiricoil uses protein domain annotation to predict coiled coil presence and oligormeric state for all completely sequenced organisms
- CC+ Archived 2011-11-08 at the PDB
- SUPERFAMILY protein domain annotation for all completely sequenced organisms based on the expertly curated SCOPcoiled coil class