Coiled coils: attractive protein folding motifs for the fabrication of self-assembled, responsive and bioactive materials

Apostolovic, Bojana; Danial, Maarten; Klok, Harm‐Anton

doi:10.1039/b914339b

Cited by 258 publications

(249 citation statements)

References 215 publications

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“…The Coiled-coil Domain Mediates Nrdp1 OligomerizationPrevious studies with a variety of proteins suggest that coiledcoil domains facilitate specific protein-protein interactions and very often mediate protein oligomerization (36,37). To determine whether the coiled-coil domain of Nrdp1 might be involved in Nrdp1 self-association, we first asked whether V5-and FLAG-tagged Nrdp1 can co-immunoprecipitate after transient co-expression in 293T cells.…”

Section: Resultsmentioning

confidence: 99%

Oligomerization of the Nrdp1 E3 Ubiquitin Ligase Is Necessary for Efficient Autoubiquitination but Not ErbB3 Ubiquitination

Printsev¹,

Yen

Sweeney

et al. 2014

Journal of Biological Chemistry

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Background: Nrdp1 ubiquitinates itself and ErbB3 to facilitate the degradation of both proteins. Result: Coiled-coil domain deletion abrogates Nrdp1 oligomerization and suppresses Nrdp1 but not ErbB3 ubiquitination and degradation. Conclusion: Oligomerization is required for efficient Nrdp1-mediated autoubiquitination but not ErbB3 ubiquitination. Significance: Nrdp1 autoubiquitination and substrate ubiquitination may be functionally separated, allowing a novel treatment strategy for breast cancer patients.

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Section: Resultsmentioning

confidence: 99%

Oligomerization of the Nrdp1 E3 Ubiquitin Ligase Is Necessary for Efficient Autoubiquitination but Not ErbB3 Ubiquitination

Printsev¹,

Yen

Sweeney

et al. 2014

Journal of Biological Chemistry

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“…Much of this type of work focuses on the use of coiledcoils in the form of leucine zippers (51). The motif we describe here may provide a useful alternative.…”

Section: Discussionmentioning

confidence: 99%

Get5 Carboxyl-terminal Domain Is a Novel Dimerization Motif That Tethers an Extended Get4/Get5 Complex

Chartron

VanderVelde

Rao

et al. 2012

Journal of Biological Chemistry

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“…38,39 Coiled coils are amongst the most ubiquitous folding motifs found in proteins and have not only been identified in the structure of proteins, but are also involved in various intracellular regulation processes. 40 They are also used as model system to study protein folding and stability due to their small size and because they have both short-range interactions which stabilize the monomeric α-helices and long-range interactions responsible for oligomeric packing. The coiled-coil peptide that we investigated was designed de novo and characterized before 41 is highly α-helical and forms 100% dimers in solution under physiological conditions.…”

Section: Coiled Coil Stabilized By Salt Bridgesmentioning

confidence: 99%

The structure of salt bridges between Arg+ and Glu− in peptides investigated with 2D-IR spectroscopy: Evidence for two distinct hydrogen-bond geometries

Huerta-Viga

Amirjalayer

Domingos

et al. 2015

The Journal of Chemical Physics

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The structure of salt bridges between Arg+ and Glu-in peptides investigated with 2D-IR spectroscopy: Evidence for two distinct hydrogen-bond geometries Huerta Viga, A.; Amirjalayer, S.; Rosa Domingos, S.M.; Meuzelaar, H.; Rupenyan, A.B.; Woutersen, S. Published in:Journal of Chemical Physics DOI:10.1063/1.4921064 Link to publication Citation for published version (APA):Huerta-Viga, A., Amirjalayer, S., Domingos, S. R., Meuzelaar, H., Rupenyan, A., & Woutersen, S. (2015). The structure of salt bridges between Arg+ and Glu-in peptides investigated with 2D-IR spectroscopy: Evidence for two distinct hydrogen-bond geometries. Journal of Chemical Physics, 142(21). DOI: 10.1063/1.4921064 General rightsIt is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. Download date: 12 May 2018THE JOURNAL OF CHEMICAL PHYSICS 142, 212444 (2015) The structure of salt bridges between Arg Salt bridges play an important role in protein folding and in supramolecular chemistry, but they are difficult to detect and characterize in solution. Here, we investigate salt bridges between glutamate (Glu − ) and arginine (Arg + ) using two-dimensional infrared (2D-IR) spectroscopy. The 2D-IR spectrum of a salt-bridged dimer shows cross peaks between the vibrational modes of Glu − and Arg + , which provide a sensitive structural probe of Glu − · · · Arg + salt bridges. We use this probe to investigate a β-turn locked by a salt bridge, an α-helical peptide whose structure is stabilized by salt bridges, and a coiled coil that is stabilized by intra-and intermolecular salt bridges. We detect a bidentate salt bridge in the β-turn, a monodentate one in the α-helical peptide, and both salt-bridge geometries in the coiled coil. To our knowledge, this is the first time 2D-IR has been used to probe tertiary side chain interactions in peptides, and our results show that 2D-IR spectroscopy is a powerful method for investigating salt bridges in solution. C 2015 Author(s). All article content, except where otherwise noted, is licensed under a Creative Commons Attribution 3.0 Unported License. [http://dx

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Coiled coils: attractive protein folding motifs for the fabrication of self-assembled, responsive and bioactive materials

Cited by 258 publications

References 215 publications

Oligomerization of the Nrdp1 E3 Ubiquitin Ligase Is Necessary for Efficient Autoubiquitination but Not ErbB3 Ubiquitination

Oligomerization of the Nrdp1 E3 Ubiquitin Ligase Is Necessary for Efficient Autoubiquitination but Not ErbB3 Ubiquitination

Get5 Carboxyl-terminal Domain Is a Novel Dimerization Motif That Tethers an Extended Get4/Get5 Complex

The structure of salt bridges between Arg+ and Glu− in peptides investigated with 2D-IR spectroscopy: Evidence for two distinct hydrogen-bond geometries

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