1bh9: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1bh9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BH9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1bh9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BH9 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PMB:PARA-MERCURY-BENZENESULFONIC+ACID'>PMB</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PMB:PARA-MERCURY-BENZENESULFONIC+ACID'>PMB</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bh9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bh9 RCSB], [http://www.ebi.ac.uk/pdbsum/1bh9 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bh9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bh9 RCSB], [http://www.ebi.ac.uk/pdbsum/1bh9 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Birck, C | [[Category: Birck, C]] | ||
[[Category: Davidson, I | [[Category: Davidson, I]] | ||
[[Category: Lavigne, A C | [[Category: Lavigne, A C]] | ||
[[Category: Mengus, G | [[Category: Mengus, G]] | ||
[[Category: Moras, D | [[Category: Moras, D]] | ||
[[Category: Poch, O | [[Category: Poch, O]] | ||
[[Category: Romier, C | [[Category: Romier, C]] | ||
[[Category: Ruff, M | [[Category: Ruff, M]] | ||
[[Category: Histone fold]] | [[Category: Histone fold]] | ||
[[Category: Htafii18]] | [[Category: Htafii18]] | ||
[[Category: Tata binding protein]] | [[Category: Tata binding protein]] | ||
[[Category: Transcription regulation complex]] | [[Category: Transcription regulation complex]] | ||
Revision as of 13:17, 22 December 2014
HTAFII18/HTAFII28 HETERODIMER CRYSTAL STRUCTURE WITH BOUND PCMBSHTAFII18/HTAFII28 HETERODIMER CRYSTAL STRUCTURE WITH BOUND PCMBS
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDetermination of the crystal structure of the human TBP-associated factor (hTAF(II))28/hTAF(II)18 heterodimer shows that these TAF(II)s form a novel histone-like pair in the TFIID complex. The histone folds in hTAF(II)28 and hTAF(II)18 were not predicted from their primary sequence, indicating that these TAF(II)s define a novel family of atypical histone fold sequences. The TAF(II)18 and TAF(II)28 histone fold motifs are also present in the N- and C-terminal regions of the SPT3 proteins, suggesting that the histone fold in SPT3 may be reconstituted by intramolecular rather than classical intermolecular interactions. The existence of additional histone-like pairs in both the TFIID and SAGA complexes shows that the histone fold is a more commonly used motif for mediating TAF-TAF interactions than previously believed. Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family.,Birck C, Poch O, Romier C, Ruff M, Mengus G, Lavigne AC, Davidson I, Moras D Cell. 1998 Jul 24;94(2):239-49. PMID:9695952[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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