Journal
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY
Volume 115, Issue 1, Pages 42-51Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.pbiomolbio.2014.02.007
Keywords
beta gamma-Crystallins; beta gamma Domain; Greek key motif; Ca2+-binding; Microbial relatives; Evolution
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Funding
- CSIR XII year network grants
- University Grant Commission
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beta gamma-Crystallins have emerged as a superfamily of structurally homologous proteins with representatives across the domains of life. A major portion of this superfamily is constituted by members from microorganisms. This superfamily has also been recognized as a novel group of Ca2+-binding proteins with huge diversity. The beta gamma domain shows variable properties in Ca2+ binding, stability and association with other domains. The various members present a series of evolutionary adaptations culminating in great diversity in properties and functions. Most of the predicted beta gamma-crystallins are yet to be characterized experimentally. In this review, we outline the distinctive features of microbial beta gamma-crystallins and their position in the beta gamma-crystallin superfamily. (C) 2014 Elsevier Ltd. All rights reserved.
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