Ontology highlight
ABSTRACT:
SUBMITTER: Srivastava SS
PROVIDER: S-EPMC4036236 | biostudies-literature | 2014 Apr
REPOSITORIES: biostudies-literature
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]