Ca2+ -binding Motif of βγ- Crystallins

被引:35
|
作者
Srivastava, Shanti Swaroop [1 ]
Mishra, Amita [1 ]
Krishnan, Bal [1 ]
Sharma, Yogendra [1 ]
机构
[1] CSIR, CCMB, Hyderabad 500007, Andhra Pradesh, India
关键词
Calcium; Calcium-binding Proteins; Crystallin; Protein Stability; Protein Structure; Beta Gamma-Crystallin; Greek Key Motif; TREFOIL FACTOR COMPLEX; DEVELOPMENT-SPECIFIC PROTEIN; SPORE COAT PROTEIN; X-RAY-ANALYSIS; CALCIUM-BINDING; MYXOCOCCUS-XANTHUS; EYE LENS; SPHERULIN; 3A; STRUCTURAL CHARACTERISTICS; AMPHIBIAN SKIN;
D O I
10.1074/jbc.O113.539569
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
-Crystallin-type double clamp (N/D)(N/D)XX(S/T)S motif is an established but sparsely investigated motif for Ca2+ binding. A -crystallin domain is formed of two Greek key motifs, accommodating two Ca2+-binding sites. -Crystallins make a separate class of Ca2+-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 Ca2+ binding to -crystallins in mediating biological processes are yet to be elucidated.
引用
收藏
页码:10958 / 10966
页数:9
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