Chaperonin
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(New page: Crystal Structure of Chaperonin, 1svt {{STRUCTURE_1svt| PDB=1svt | SIZE=300| SCENE= |right|CAPTION=GroEL/GroES complex, 1svt }} Chaperonin (C...)
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Revision as of 07:46, 21 April 2011
Image:1svt.png
Crystal Structure of Chaperonin, 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.
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3D Structures of Chaperonin
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Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Eric Martz, Jaime Prilusky
