Cited 0 time in webofscience Cited 0 time in scopus

Recent advances in NMR-based structural characterization of αB-crystallin and its potential role in human diseases

Title
Recent advances in NMR-based structural characterization of αB-crystallin and its potential role in human diseases
Authors
Muniyappan, SrinivasanKim, Jin Hae
DGIST Authors
Muniyappan, Srinivasan; Kim, Jin Hae
Issue Date
2019-03
Citation
Journal of the Korean Magnetic Resonance Society, 23(1), 26-32
Type
Article
Article Type
Article
Author Keywords
αB-crystallinsmall heat-shock proteinchaperoneprotein structureNMR spectroscopy
ISSN
1226-6531
Abstract
αB-crystallin (αBC) is a member of a small heat-shock protein (sHSP) superfamily and plays a predominant role in cellular protein homeostasis network by rescuing misfolded proteins from irreversible aggregation. αBC assembles into dynamic and polydisperse high molecular weight complexes containing 12 to 48 monomers; this variable stereochemistry of αBC has been linked to quaternary subunit exchange and its chaperone activity. The chaperone activity of αBC poses great potential as therapeutic agents for various neurodegenerative diseases. In this mini-review, we briefly outline the recent advancement in structural characterization of αBCs and its potential role to inhibit protein misfolding and aggregation in various human diseases. In particular, nuclear magnetic resonance (NMR) spectroscopy and its complimentary techniques have contributed much to elucidate highly-dynamic nature of αBCs, among which notable advancements are discussed in detail. We highlight the importance of resolving the structural details of various αBC oligomers, their quaternary dynamics, and structural heterogeneity.
URI
http://hdl.handle.net/20.500.11750/9684
DOI
10.6564/JKMRS.2019.23.1.026
Publisher
한국자기공명학회
Related Researcher
Files:
There are no files associated with this item.
Collection:
Department of New BiologyProtein Structure Aging Laboratory1. Journal Articles


qrcode mendeley

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE