1M62
Solution structure of the BAG domain from BAG4/SODD
Summary for 1M62
| Entry DOI | 10.2210/pdb1m62/pdb |
| Related | 1HX1 1I6Z |
| Descriptor | BAG-family molecular chaperone regulator-4 (1 entity in total) |
| Functional Keywords | bag domain, bag4, sodd, silencer of death domains, hsp70/hsc70 co-chaperone, chaperone |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: O95429 |
| Total number of polymer chains | 1 |
| Total formula weight | 9973.53 |
| Authors | Briknarova, K.,Takayama, S.,Homma, S.,Baker, K.,Cabezas, E.,Hoyt, D.W.,Li, Z.,Satterthwait, A.C.,Ely, K.R. (deposition date: 2002-07-11, release date: 2002-07-24, Last modification date: 2024-05-22) |
| Primary citation | Briknarova, K.,Takayama, S.,Homma, S.,Baker, K.,Cabezas, E.,Hoyt, D.W.,Li, Z.,Satterthwait, A.C.,Ely, K.R. BAG4/SODD protein contains a short BAG domain. J.Biol.Chem., 277:31172-31178, 2002 Cited by PubMed Abstract: 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, 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. PubMed: 12058034DOI: 10.1074/jbc.M202792200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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