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Ca2+-binding motif of ??-crystallins.


ABSTRACT: ??-Crystallin-type double clamp (N/D)(N/D)XX(S/T)S motif is an established but sparsely investigated motif for Ca(2+) binding. A ??-crystallin domain is formed of two Greek key motifs, accommodating two Ca(2+)-binding sites. ??-Crystallins make a separate class of Ca(2+)-binding proteins (CaBP), apparently a major group of CaBP in bacteria. Paralleling the diversity in ??-crystallin domains, these motifs also show great diversity, both in structure and in function. Although the expression of some of them has been associated with stress, virulence, and adhesion, the functional implications of Ca(2+) binding to ??-crystallins in mediating biological processes are yet to be elucidated.

SUBMITTER: Srivastava SS 

PROVIDER: S-EPMC4036236 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

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Ca2+-binding motif of βγ-crystallins.

Srivastava Shanti Swaroop SS   Mishra Amita A   Krishnan Bal B   Sharma Yogendra Y  

The Journal of biological chemistry 20140224 16


βγ-Crystallin-type double clamp (N/D)(N/D)XX(S/T)S motif is an established but sparsely investigated motif for Ca(2+) binding. A βγ-crystallin domain is formed of two Greek key motifs, accommodating two Ca(2+)-binding sites. βγ-Crystallins make a separate class of Ca(2+)-binding proteins (CaBP), apparently a major group of CaBP in bacteria. Paralleling the diversity in βγ-crystallin domains, these motifs also show great diversity, both in structure and in function. Although the expression of som  ...[more]

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