Chaperonin

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E. coli GroEL (green)/GroES (magenta) complex with ADP, AlF3, Mg+2 and K+ ions (PDB entry 1pcq)

3D Structures of Chaperonin

Updated on 20-October-2017

See Heat Shock Proteins

References

  1. Apetri AC, Horwich AL. Chaperonin chamber accelerates protein folding through passive action of preventing aggregation. Proc Natl Acad Sci U S A. 2008 Nov 11;105(45):17351-5. doi:, 10.1073/pnas.0809794105. Epub 2008 Nov 5. PMID:18987317 doi:http://dx.doi.org/10.1073/pnas.0809794105
  2. Ditzel L, Lowe J, Stock D, Stetter KO, Huber H, Huber R, Steinbacher S. Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell. 1998 Apr 3;93(1):125-38. PMID:9546398
  3. Leitner A, Joachimiak LA, Bracher A, Monkemeyer L, Walzthoeni T, Chen B, Pechmann S, Holmes S, Cong Y, Ma B, Ludtke S, Chiu W, Hartl FU, Aebersold R, Frydman J. The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT. Structure. 2012 May 9;20(5):814-25. Epub 2012 Apr 12. PMID:22503819 doi:10.1016/j.str.2012.03.007

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