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The Journal of biological chemistry, 2002-08, Vol.277 (34), p.31172-31178
Ort / Verlag
United States: American Society for Biochemistry and Molecular Biology
Erscheinungsjahr
2002
Quelle
Free E-Journal (出版社公開部分のみ)
Beschreibungen/Notizen
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 (Briknarová, 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., Llinás, M., Reed, J. C.,
and Ely, K. R. (2001) Nat. Struct. Biol. 8, 349â352). 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.