Abstract:
:Small heat shock proteins are ubiquitous molecular chaperones that form the first line of defence against the detrimental effects of cellular stress. Under conditions of stress they undergo drastic conformational rearrangements in order to bind to misfolded substrate proteins and prevent cellular protein aggregation. Owing to the dynamic nature of small heat shock protein oligomers, elucidating the structural basis of chaperone action and oligomerization still remains a challenge. In order to understand the organization of sHSP oligomers, we have determined crystal structures of a small heat shock protein from Salmonella typhimurium in a dimeric form and two higher oligomeric forms: an 18-mer and a 24-mer. Though the core dimer structure is conserved in all the forms, structural heterogeneity arises due to variation in the terminal regions.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Mani N,Bhandari S,Moreno R,Hu L,Prasad BVV,Suguna Kdoi
10.1038/srep24019subject
Has Abstractpub_date
2016-04-07 00:00:00pages
24019issn
2045-2322pii
srep24019journal_volume
6pub_type
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