Skip to main content
Log in

Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1

  • NMR structure note
  • Published:
Journal of Biomolecular NMR Aims and scope Submit manuscript

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5

References

  • Bagneris C, Bateman OA et al (2009) Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20. J Mol Biol 392(5):1242–1252

    Article  Google Scholar 

  • Baldwin AJ, Lioe H et al (2011) The polydispersity of alphaB-crystallin is rationalized by an interconverting polyhedral architecture. Structure 19(12):1855–1863

    Article  Google Scholar 

  • Baranova EV, Weeks SD et al (2011) Three-dimensional structure of alpha-crystallin domain dimers of human small heat shock proteins HSPB1 and HSPB6. J Mol Biol 411(1):110–122

    Article  Google Scholar 

  • Braun N, Zacharias M et al (2011) Multiple molecular architectures of the eye lens chaperone alphaB-crystallin elucidated by a triple hybrid approach. Proc Natl Acad Sci USA 108(51):20491–20496

    Article  ADS  Google Scholar 

  • Chalova AS, Sudnitsyna MV et al (2014) Effect of disulfide crosslinking on thermal transitions and chaperone-like activity of human small heat shock protein HspB1. Cell Stress Chaperones 19(6):963–972

    Article  Google Scholar 

  • Clark AR, Naylor CE et al (2011) Crystal structure of R120G disease mutant of human alphaB-crystallin domain dimer shows closure of a groove. J Mol Biol 408(1):118–134

    Article  Google Scholar 

  • Delaglio F, Grzesiek S et al (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3):277–293

    Google Scholar 

  • Gorman AM, Szegezdi E et al (2005) Hsp27 inhibits 6-hydroxydopamine-induced cytochrome c release and apoptosis in PC12 cells. Biochem Biophys Res Commun 327(3):801–810

    Article  Google Scholar 

  • Graumann J, Lilie H et al (2001) Activation of the redox-regulated molecular chaperone Hsp33—a two-step mechanism. Structure 9(5):377–387

    Article  Google Scholar 

  • Hochberg GK, Ecroyd H et al (2014) The structured core domain of alphaB-crystallin can prevent amyloid fibrillation and associated toxicity. Proc Natl Acad Sci USA 111(16):E1562–E1570

    Article  ADS  Google Scholar 

  • Jehle S, van Rossum B et al (2009) alphaB-crystallin: a hybrid solid-state/solution-state NMR investigation reveals structural aspects of the heterogeneous oligomer. J Mol Biol 385(5):1481–1497

    Article  Google Scholar 

  • Jehle S, Vollmar BS et al (2011) N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. Proc Natl Acad Sci USA 108(16):6409–6414

    Article  ADS  Google Scholar 

  • Johnson BA (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol Biol 278:313–352

    Google Scholar 

  • Kriehuber T, Rattei T et al (2010) Independent evolution of the core domain and its flanking sequences in small heat shock proteins. FASEB J 24(10):3633–3642

    Article  Google Scholar 

  • Laganowsky A, Benesch JL et al (2010) Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function. Protein Sci 19(5):1031–1043

    Article  Google Scholar 

  • Peschek J, Braun N et al (2013) Regulated structural transitions unleash the chaperone activity of alphaB-crystallin. Proc Natl Acad Sci USA 110(40):E3780–E3789

    Article  ADS  Google Scholar 

  • Sgourakis NG, Lange OF et al (2011) Determination of the structures of symmetric protein oligomers from NMR chemical shifts and residual dipolar couplings. J Am Chem Soc 133(16):6288–6298

    Article  Google Scholar 

  • Wishart DS, Bigam CG et al (1995) 1H, 13C and 15 N chemical shift referencing in biomolecular NMR. J Biomol NMR 6(2):135–140

    Google Scholar 

Download references

Acknowledgments

We thank David Baker for access to RosettaOligomer software and computing facilities, William Atkins for use of his fluorimeter, and Hannah Baughman for help with fluorescence experiments. The work was supported by NIH Grant 1R01 EY017370 (to REK).

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Rachel E. Klevit.

Electronic supplementary material

Below is the link to the electronic supplementary material.

Supplementary material 1 (PDF 387 kb)

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Rajagopal, P., Liu, Y., Shi, L. et al. Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1. J Biomol NMR 63, 223–228 (2015). https://doi.org/10.1007/s10858-015-9973-0

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10858-015-9973-0

Keywords

Navigation