Abstract:
:Although proteins belonging to the sHSP superfamily are diverse in sequence and size, most share characteristic features, including 1) a small molecular mass of 12-43 kDa, 2) a conserved alpha-crystallin domain of 80-100 residues, 3) formation of large oligomers, 4) a dynamic quaternary structure, and 5) induction by stress conditions and chaperone activity in suppressing protein aggregation. HSPB2/MKBP (myotonic dystrophy kinase-bind-protein) retains the structural motif of the alpha-crystallin family of HSPs but shows a unique nature compared with canonical family members, characterized by gene allocation, specific binding partners in skeletal muscle, and unique stress responsiveness. MKBP may be involved in the pathogenesis of myotonic dystrophy and contribute to the neuropathology in both Alzheimer's disease and hereditary cerebral hemorrhage with amyloidosis, Dutch type.
journal_name
J Neurosci Resjournal_title
Journal of neuroscience researchauthors
Hu Z,Yang B,Lu W,Zhou W,Zeng L,Li T,Wang Xdoi
10.1002/jnr.21682subject
Has Abstractpub_date
2008-08-01 00:00:00pages
2125-33issue
10eissn
0360-4012issn
1097-4547journal_volume
86pub_type
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