Sandbox Reserved 820: Difference between revisions

From Proteopedia
Jump to navigationJump to search
mNo edit summary
No edit summary
Line 19: Line 19:


Each monomer is divided in <scene name='56/568018/Monomer_structure/5'>3 thioredoxin domains (TRX)</scene>: <scene name='56/568018/Monomer_structure/7'>the N-term</scene>, <scene name='56/568018/Monomer_structure/6'>the middle</scene> and the <scene name='56/568018/Monomer_structure/8'>C-term</scene> domains. Each of these has a regular structure: a <scene name='56/568018/Beta_sheet/4'>5 strands beta sheet core</scene>  surrounded by <scene name='56/568018/Alpha_helix/3'>4 alpha helices</scene>.  
Each monomer is divided in <scene name='56/568018/Monomer_structure/5'>3 thioredoxin domains (TRX)</scene>: <scene name='56/568018/Monomer_structure/7'>the N-term</scene>, <scene name='56/568018/Monomer_structure/6'>the middle</scene> and the <scene name='56/568018/Monomer_structure/8'>C-term</scene> domains. Each of these has a regular structure: a <scene name='56/568018/Beta_sheet/4'>5 strands beta sheet core</scene>  surrounded by <scene name='56/568018/Alpha_helix/3'>4 alpha helices</scene>.  
Usually these domains are involved in redox phenomena, which lead to disulfide bounds creation. Here these domains are inactive but play an important role in the polymerization of CASQ2.
Usually these domains are involved in redox phenomena, which lead to disulfide bounds creation. Here these domains are inactive but play an important role in the polymerization of CASQ2.<ref name="Monomère structure">http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?ascbin=8&maxaln=10&seltype=2&uid=239372&querygi=429544235&aln=1,227,0,109</ref>


=== Polymer Structure ===   
=== Polymer Structure ===