| Literature DB >> 24594023 |
Amita Mishra1, Bal Krishnan1, Shanti Swaroop Srivastava1, Yogendra Sharma2.
Abstract
βγ-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 Ca(2+)-binding proteins with huge diversity. The βγ domain shows variable properties in Ca(2+) 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 βγ-crystallins are yet to be characterized experimentally. In this review, we outline the distinctive features of microbial βγ-crystallins and their position in the βγ-crystallin superfamily.Entities:
Keywords: Ca(2+)-binding; Evolution; Greek key motif; Microbial relatives; βγ Domain; βγ-Crystallins
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Year: 2014 PMID: 24594023 DOI: 10.1016/j.pbiomolbio.2014.02.007
Source DB: PubMed Journal: Prog Biophys Mol Biol ISSN: 0079-6107 Impact factor: 3.667