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[[Image: | ==TFIIIA FINGER 1-3 BOUND TO DNA, NMR, 22 STRUCTURES== | ||
<StructureSection load='1tf3' size='340' side='right' caption='[[1tf3]], [[NMR_Ensembles_of_Models | 22 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1tf3]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TF3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TF3 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> | |||
<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=1tf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tf3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tf3 RCSB], [http://www.ebi.ac.uk/pdbsum/1tf3 PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tf/1tf3_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The three N-terminal zinc fingers of transcription factor IIIA bind in the DNA major groove. Substantial packing interfaces are formed between adjacent fingers, the linkers lose their intrinsic flexibility upon DNA binding, and several lysine side chains implicated in DNA recognition are dynamically disordered. | |||
Domain packing and dynamics in the DNA complex of the N-terminal zinc fingers of TFIIIA.,Foster MP, Wuttke DS, Radhakrishnan I, Case DA, Gottesfeld JM, Wright PE Nat Struct Biol. 1997 Aug;4(8):605-8. PMID:9253405<ref>PMID:9253405</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
[[Category: Case, D A.]] | [[Category: Case, D A.]] | ||
Revision as of 00:09, 30 September 2014
TFIIIA FINGER 1-3 BOUND TO DNA, NMR, 22 STRUCTURESTFIIIA FINGER 1-3 BOUND TO DNA, NMR, 22 STRUCTURES
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 PubMedThe three N-terminal zinc fingers of transcription factor IIIA bind in the DNA major groove. Substantial packing interfaces are formed between adjacent fingers, the linkers lose their intrinsic flexibility upon DNA binding, and several lysine side chains implicated in DNA recognition are dynamically disordered. Domain packing and dynamics in the DNA complex of the N-terminal zinc fingers of TFIIIA.,Foster MP, Wuttke DS, Radhakrishnan I, Case DA, Gottesfeld JM, Wright PE Nat Struct Biol. 1997 Aug;4(8):605-8. PMID:9253405[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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