Ca2+-binding motif of ßγ-crystallins.
J Biol Chem
; 289(16): 10958-10966, 2014 Apr 18.
Article
em En
| MEDLINE
| ID: mdl-24567326
ßγ-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 ßγ-crystallin domain is formed of two Greek key motifs, accommodating two Ca(2+)-binding sites. ßγ-Crystallins make a separate class of Ca(2+)-binding proteins (CaBP), apparently a major group of CaBP in bacteria. Paralleling the diversity in ßγ-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 ßγ-crystallins in mediating biological processes are yet to be elucidated.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Bactérias
/
Proteínas de Bactérias
/
Proteínas de Ligação ao Cálcio
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Cálcio
/
Beta-Cristalinas
/
Gama-Cristalinas
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article