Template:SGC BRD3: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Eran Hodis (talk | contribs) m Protected "Template:SGC BRD3" [edit=sysop:move=sysop] |
Eran Hodis (talk | contribs) No edit summary |
||
| Line 1: | Line 1: | ||
<!--The content between the words START_SGC and END_SGC falls under the copyright specified by the Structural Genomics Consortium at Oxford, and not under the GNU Free Document License that applies to all user-added content on Proteopedia. Please be aware of this. --> | |||
<!--START_SGC--> | |||
===An SGC Structure=== | ===An SGC Structure=== | ||
| Line 16: | Line 19: | ||
=== Structural features === | === Structural features === | ||
<applet load='2nxb' size='500' frame='true' align='right' caption='Human [[Human bromodomain containing protein|BRD3]] ' /> | <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 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. | ||
| Line 32: | Line 35: | ||
=== References === | === References === | ||
<ref group='xtra'>PMID:15128596</ref><ref group='xtra'>PMID:16008511</ref><ref group='xtra'>PMID:16928766</ref><ref group='xtra'>PMID:9373153</ref><ref group='xtra'>PMID:12600283</ref><references group='xtra'/> | <ref group='xtra'>PMID:15128596</ref><ref group='xtra'>PMID:16008511</ref><ref group='xtra'>PMID:16928766</ref><ref group='xtra'>PMID:9373153</ref><ref group='xtra'>PMID:12600283</ref><references group='xtra'/> | ||
<!--END_SGC--> | |||
