Sandbox Naama
From Proteopedia
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The uniqe structure of the mamalian chaperonine TRic/CCT was first published in 2010 by Cong Y et al<ref>pmid:020194787</ref>. it was determined in a low resolution of 4.7 A by cryo-EM. It is composed of <scene name='Sandbox_Naama/Tric_dimer/1'> two identical heterooligomer </scene> ring shaped subunits consisting of eight different paralogous subunits <scene name='Sandbox_Naama/One_subunit/2'>view one subunit</scene> /<scene name='Sandbox_Naama/Colored_tric/1'>view full protein</scene> | The uniqe structure of the mamalian chaperonine TRic/CCT was first published in 2010 by Cong Y et al<ref>pmid:020194787</ref>. it was determined in a low resolution of 4.7 A by cryo-EM. It is composed of <scene name='Sandbox_Naama/Tric_dimer/1'> two identical heterooligomer </scene> ring shaped subunits consisting of eight different paralogous subunits <scene name='Sandbox_Naama/One_subunit/2'>view one subunit</scene> /<scene name='Sandbox_Naama/Colored_tric/1'>view full protein</scene> | ||
| - | Cong et al discovered that this chaperonine functions | ||
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| - | <scene name='Sandbox_Naama/Colored_tric/1'>Click here to see TRic colored by chains</scene> | ||
Revision as of 14:15, 6 September 2012
The Eukaryotic Chaperonin TRiC/CCT
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- ↑ Cong Y, Baker ML, Jakana J, Woolford D, Miller EJ, Reissmann S, Kumar RN, Redding-Johanson AM, Batth TS, Mukhopadhyay A, Ludtke SJ, Frydman J, Chiu W. 4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement. Proc Natl Acad Sci U S A. 2010 Mar 1. PMID:20194787
