Sandbox Reserved 820: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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 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>.<ref name="Martin">PMID:7788290</ref>
 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="Monomere structure">NCBI Structure Ressource: CASQ2 calsequestrin 2  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>
-Finally, the C-term Asp-rich extremity  is intrisically disordered ''(as a consequence, the C-term extrimity cannot be represented in 3D structures)''.
+Finally, the C-term Asp-rich extremity  is intrisically disordered ''(therefore, the C-term extrimity cannot be represented in 3D structures)''.
 === Polymer Structure ===
 Within the sarcoplasmic reticulum (SR) lumen, CASQ2 polymerizes to form <scene name='56/568018/Dimer/1'>homodimers</scene>, homotetramers and