This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1x41
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Solution structure of the Myb-like DNA binding domain of human Transcriptional adaptor 2-like, isoform B== | ==Solution structure of the Myb-like DNA binding domain of human Transcriptional adaptor 2-like, isoform B== | ||
| - | <StructureSection load='1x41' size='340' side='right'caption='[[1x41 | + | <StructureSection load='1x41' size='340' side='right'caption='[[1x41]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1x41]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1x41]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X41 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X41 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1x41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x41 OCA], [https://pdbe.org/1x41 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x41 RCSB], [https://www.ebi.ac.uk/pdbsum/1x41 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x41 ProSAT], [https://www.topsan.org/Proteins/RSGI/1x41 TOPSAN]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1x41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x41 OCA], [https://pdbe.org/1x41 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x41 RCSB], [https://www.ebi.ac.uk/pdbsum/1x41 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x41 ProSAT], [https://www.topsan.org/Proteins/RSGI/1x41 TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/TAD2A_HUMAN TAD2A_HUMAN] Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. Required for the function of some acidic activation domains, which activate transcription from a distant site (By similarity). Binds double-stranded DNA. Binds dinucleosomes, probably at the linker region between neighboring nucleosomes. Plays a role in chromatin remodeling.<ref>PMID:19103755</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 23: | Line 23: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Inoue | + | [[Category: Inoue M]] |
| - | [[Category: Kigawa | + | [[Category: Kigawa T]] |
| - | [[Category: Koshiba | + | [[Category: Koshiba S]] |
| - | + | [[Category: Sasagawa A]] | |
| - | [[Category: Sasagawa | + | [[Category: Sato M]] |
| - | [[Category: Sato | + | [[Category: Yokoyama S]] |
| - | [[Category: Yokoyama | + | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Solution structure of the Myb-like DNA binding domain of human Transcriptional adaptor 2-like, isoform B
| |||||||||||
Categories: Homo sapiens | Large Structures | Inoue M | Kigawa T | Koshiba S | Sasagawa A | Sato M | Yokoyama S

