1m62
From Proteopedia
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Solution structure of the BAG domain from BAG4/SODD
Overview
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 (Briknarova, 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.
About this Structure
1M62 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
BAG4/SODD protein contains a short BAG domain., Briknarova K, Takayama S, Homma S, Baker K, Cabezas E, Hoyt DW, Li Z, Satterthwait AC, Ely KR, J Biol Chem. 2002 Aug 23;277(34):31172-8. Epub 2002 Jun 10. PMID:12058034
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