Chaperonin

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Revision as of 07:46, 21 April 2011 by Michal Harel (talk | contribs) (New page: left|200px|thumb|Crystal Structure of Chaperonin, [[1svt]] {{STRUCTURE_1svt| PDB=1svt | SIZE=300| SCENE= |right|CAPTION=GroEL/GroES complex, 1svt }} Chaperonin (C...)
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File:1svt.png
Crystal Structure of Chaperonin, 1svt

Template:STRUCTURE 1svt

Chaperonin (CPN) are oligomeric proteins which mediate the folding of polypeptide chains. Group I CPNs are found in bacteria, chloroplasts and mitochondria. They include the most characterized GroEL/GroES complex from Escherichia coli and CPN60/CPN10 from Thermus thermophilus. The larger subunit (GroEL, CPN60) contains 3 domains. The apical domain is the one which binds the substrate. Group II CPNs are found in eukaryotic cytosol and archaea. Thermosome is a CPN complex found in archaea. CCT is a CPN complex found in eukarya.

3D Structures of Chaperonin

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