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 superimpose 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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(TIP: <scene name='Template:SGC_BRD3/Sgc_brd3_scene_3/1'>reset</scene>the view)

The interface between both BRD3 BD1 monomers covers a large mainly hydrophobic surface area suggesting that this domain might be dimeric in solution. Dimerization of bromo domains has also been suggested for the closely related protein BRD2. However, the interface which is formed in BRD2 by the two C-terminal helices is not conserved in BRD3. As expected from their high degrees of sequence conservation (78% identity) the overall fold of BRD3 is closely related to the bromo domain of BRD2 (r.m.s.d 0.7 Å between chain B BRD3 and chain A BRD2; pdb-code: [[1x0j]]).

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 superimpose 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}})
-(TIP: reset the view)
+(TIP: <scene name='Template:SGC_BRD3/Sgc_brd3_scene_3/1'>reset</scene>the view)
 The interface between both BRD3 BD1 monomers covers a large mainly hydrophobic surface area suggesting that this domain might be dimeric in solution. Dimerization of bromo domains has also been suggested for the closely related protein BRD2. However, the interface which is formed in BRD2 by the two C-terminal helices is not conserved in BRD3. As expected from their high degrees of sequence conservation (78% identity) the overall fold of BRD3 is closely related to the bromo domain of BRD2 (r.m.s.d 0.7 Å between chain B BRD3 and chain A BRD2; pdb-code: [[1x0j]]).