Structural investigation of human small heat shock proteins alpha-beta-crystallin and HSP27.
EMSL Project ID
25707
Abstract
In response to stress, the family of proteins known collectively as small heat shock proteins (sHsp) may comprise as much as 1% of the total cellular protein. Found in all organisms from bacteria to humans, sHSPs act to sequester partly unfolded proteins to protect them from further unfolding and detrimental aggregation, processes which, if allowed to proceed unchecked, may trigger cell death. Although it is clear that sHSPs play a critical role in an organisms ability to survive stress, details of the biological roles for specific sHsps are only now beginning to emerge. There are ten sHsps predicted in the human genome and their expression is tissue-specific, suggesting that each has evolved to respond to specific stress needs of the tissues in which they are found. We propose to study the structure and dynamics of two human sHsps, αB-crystallin and HSP27, in their smallest homodimeric forms and in their large molecular assemblies using solutions-state and solid-state NMR approaches.
Project Details
Project type
Large-Scale EMSL Research
Start Date
2007-05-23
End Date
2010-09-30
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members
Related Publications
Jehle S, B van Rossum, JR Stout, SM Noguchi, K Falber, K Rehbein, H Oschkinat, RE Klevit, and P Rajagopal. 2009. "?B-Crystallin: A Hybrid Solid-State/Solution-State NMR Investigation Reveals Structural Aspects of the Heterogeneous Oligomer." Journal of Molecular Biology 385(5):1482-1497. doi:10.1016/j.jmb.2008.10.097