BAG4/SODD protein contains a short BAG domain
BAG4/SODD protein contains a short BAG domain
复制标题
DOI：
10.1074/jbc.m202792200
复制
发表时间：
2002-08-23
影响因子：
4.8
通讯作者：
Ely, KR
中科院分区：
文献类型：
--
作者：
Briknarová, K;Takayama, S;Ely, KR
BAG（Bcl-2-associated athanogene）蛋白是影响多种细胞途径的分子伴侣调节剂。所有成员都有一个保守的基序，称为BAG结构域（BD），它与Hsp 70/Hsc 70家族蛋白结合并调节其活性。我们已经通过多维核磁共振方法确定了来自BAG 4/SODD（死亡结构域的沉默物）的BD的溶液结构，并将其与BAG 1中的相应结构域进行了比较（Briknarovi，K.，Takayama，S.，布里夫湖Havert，M. L.，膝，D. A.、Velasco，J.，Homma，S.，Cabezas，E.，斯图尔特，J.，霍伊特，D. W.，Satterthwait，A. C.的方法，Llinas，M.，Reed，J.C.，和伊利，K. R.（2001）Nat.Struct.Biol.8，349-352）。来自这两种BAG蛋白的BD之间的差异是惊人的，并且结构比较定义了哺乳动物含BD蛋白的两个亚家族。一个亚家族包括密切相关的BAG 3、BAG 4和BAG 5蛋白，另一个由BAG 1代表，其包含结构和进化上不同的BD。BAG 1和BAG 4的BD都是三螺旋束;然而，在BAG 4中，该束中的每个螺旋比BAG 1中的对应物短三到四圈，这使结构域的长度减少了三分之一。因此，BAG 4 BD代表了能够结合Hsc 70并调节其分子伴侣活性的最小功能片段的原型。
BAG (Bcl-2-associated athanogene) proteins are molecular chaperone regulators that affect diverse cellular pathways. All members share a conserved motif, called the BAG domain (BD), which binds to Hsp70/Hsc70 family proteins and modulates their activity. We have determined the solution structure of BD from BAG4/SODD (silencer of death domains) by multidimensional nuclear magnetic resonance methods and compared it to the corresponding domain in BAG1 (Briknarovi, K., Takayama, S., Brive, L., Havert, M. L., Knee, D. A., Velasco, J., Homma, S., Cabezas, E., Stuart, J., Hoyt, D. W., Satterthwait, A. C., Llinas, M., Reed, J. C., and Ely, K. R. (2001) Nat. Struct. Biol. 8, 349-352). The difference between BDs from these two BAG proteins is striking, and the structural comparison defines two subfamilies of mammalian BD-containing proteins. One subfamily includes the closely related BAG3, BAG4, and BAG5 proteins, and the other is represented by BAG1, which contains a structurally and evolutionarily distinct BD. BDs from both BAG1 and BAG4 are three-helix bundles; however, in BAG4, each helix in this bundle is three to four turns shorter than its counterpart in BAG1, which reduces the length of the domain by one-third. BAG4 BD thus represents a prototype of the minimal functional fragment that is capable of binding to Hsc70 and modulating its chaperone activity.