Template:SGC BRD3: Difference between revisions

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=== Structural features ===

The structures of BRD3 discussed here comprises two independent structures of the first bromo domain (BD1) including the sequence between residue Glu25 and Glu144 as well as the second bromo domain (BD2) (residues Lys307-Pro416). The <scene name='Template:SGC_BRD3/Sgc_brd3_scene_1/2'>asymmetric unit</scene> of BD1 contains two protein molecules in addition to one sodium ion and 7 ethylene glycole molecules used as a cryo protecting agent. Both BD1 molecules present in the asymmetric unit <scene name='Template:SGC_BRD3/Sgc_brd3_scene2/1'>superimpose</scene>with an r.m.s.d. of ~1Å. The main structural differences are located in the large loop region connecting helix 1 with helix 2 (Asp64-Lys78) which is involved in the binding of acetylated lysine containing sequences. The N-terminal residues Glu25-Gly333 were only visible in chain A.

The structures of BRD3 discussed here comprises two independent structures of the first bromo domain (BD1) including the sequence between residue Glu25 and Glu144 as well as the second bromo domain (BD2) (residues Lys307-Pro416). The <scene name='Template:SGC_BRD3/Sgc_brd3_scene_1/2'>asymmetric unit</scene> of BD1 contains two protein molecules in addition to one sodium ion and 7 ethylene glycole molecules used as a cryo protecting agent. Both BD1 molecules present in the asymmetric unit <scene name='Template:SGC_BRD3/Sgc_brd3_scene2/1'>superimpose</scene> with an r.m.s.d. of ~1Å. The main structural differences are located in the large loop region connecting helix 1 with helix 2 (Asp64-Lys78) which is involved in the binding of acetylated lysine containing sequences. The N-terminal residues Glu25-Gly333 were only visible in chain A.

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Template:SGC BRD3: Difference between revisions

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 === Structural features ===
 <applet load='2nxb' size='500' frame='true' align='right' caption='Human [[Human bromodomain containing protein 3|BRD3]] ' />
-The structures of BRD3 discussed here comprises two independent structures of the first bromo domain (BD1) including the sequence between residue Glu25 and Glu144 as well as the second bromo domain (BD2) (residues Lys307-Pro416). The <scene name='Template:SGC_BRD3/Sgc_brd3_scene_1/2'>asymmetric unit</scene> of BD1 contains two protein molecules in addition to one sodium ion and 7 ethylene glycole molecules used as a cryo protecting agent. Both BD1 molecules present in the asymmetric unit <scene name='Template:SGC_BRD3/Sgc_brd3_scene2/1'>superimpose</scene>with an r.m.s.d. of ~1Å. The main structural differences are located in the large loop region connecting helix 1 with helix 2 (Asp64-Lys78) which is involved in the binding of acetylated lysine containing sequences. The N-terminal residues Glu25-Gly333 were only visible in chain A.
+The structures of BRD3 discussed here comprises two independent structures of the first bromo domain (BD1) including the sequence between residue Glu25 and Glu144 as well as the second bromo domain (BD2) (residues Lys307-Pro416). The <scene name='Template:SGC_BRD3/Sgc_brd3_scene_1/2'>asymmetric unit</scene> of BD1 contains two protein molecules in addition to one sodium ion and 7 ethylene glycole molecules used as a cryo protecting agent. Both BD1 molecules present in the asymmetric unit <scene name='Template:SGC_BRD3/Sgc_brd3_scene2/1'>superimpose</scene> with an r.m.s.d. of ~1Å. The main structural differences are located in the large loop region connecting helix 1 with helix 2 (Asp64-Lys78) which is involved in the binding of acetylated lysine containing sequences. The N-terminal residues Glu25-Gly333 were only visible in chain A.
 (TIP: the background colour can be changed to {{Template:Button Set White Background}} or {{Template:Button Set Black Background}})