Chloride Intracellular Channel Protein 2: Difference between revisions
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CLIC2 protein is composed of this GST fold and also of two other domains: an N-terminal domain and a C-terminal domain. The <scene name='Sandbox123/N-term_clic2/1'>N-terminal domain</scene>(residues 1-94) has a thioredoxin-like fold made of four-stranded mixed β-sheets and two α-helices running parallel with the sheet of one face (α1 and α3) and one helix (α2) running perpendicular to the sheet on the other face (β α β α β β). | CLIC2 protein is composed of this GST fold and also of two other domains: an N-terminal domain and a C-terminal domain. The <scene name='Sandbox123/N-term_clic2/1'>N-terminal domain</scene>(residues 1-94) has a thioredoxin-like fold made of four-stranded mixed β-sheets and two α-helices running parallel with the sheet of one face (α1 and α3) and one helix (α2) running perpendicular to the sheet on the other face (β α β α β β). | ||
The C-terminal domain (residues 107-245) is exclusively helical composed. It contains a long loop (residues 152-180) between helices 5 and 6, which is a characteristic of the CLIC family wich is called the <scene name='Sandbox123/Foot_loop/1'>foot loop</scene>. | The <scene name='Sandbox123/C-term_clic2/1'>C-terminal domain</scene>(residues 107-245) is exclusively helical composed. It contains a long loop (residues 152-180) between helices 5 and 6, which is a characteristic of the CLIC family wich is called the <scene name='Sandbox123/Foot_loop/1'>foot loop</scene>. | ||
Those two domains are linked by an interdomain loop (residues 95–106) rich in proline residues (more than 33% of proline). Actually there are | Those two domains are linked by an interdomain loop (residues 95–106) rich in proline residues (more than 33% of proline). Actually there are | ||
<scene name='Sandbox123/Two_diprolines/1'>two diproline</scene>, Pro70-Pro71 and Pro96-Pro97 in this loop wich is called <scene name='Sandbox123/Joint_loop/2'>joint loop</scene>. Those diprolines lead to direction changing in the peptide chain. The largest deviations in the N-terminal domain occurs between the residues 55 and 69 that implie helix α2 and its surrounding sequences and also a loop (residues 80-84) that bind the β-strand 4 to helix α3. | <scene name='Sandbox123/Two_diprolines/1'>two diproline</scene>, Pro70-Pro71 and Pro96-Pro97 in this loop wich is called <scene name='Sandbox123/Joint_loop/2'>joint loop</scene>. Those diprolines lead to direction changing in the peptide chain. The largest deviations in the N-terminal domain occurs between the residues 55 and 69 that implie helix α2 and its surrounding sequences and also a loop (residues 80-84) that bind the β-strand 4 to helix α3. | ||
