1pue
From Proteopedia
(Difference between revisions)
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<StructureSection load='1pue' size='340' side='right'caption='[[1pue]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1pue' size='340' side='right'caption='[[1pue]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1pue]] is a 6 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1pue]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PUE FirstGlance]. <br> |
- | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=1pue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pue OCA], [https://pdbe.org/1pue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pue RCSB], [https://www.ebi.ac.uk/pdbsum/1pue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pue ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
- | [ | + | [https://www.uniprot.org/uniprot/SPI1_MOUSE SPI1_MOUSE] Note=Involved in murine acute Friend erythroleukemia. It is a target region for SFFV proviral insertion. |
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/SPI1_MOUSE SPI1_MOUSE] Binds to the PU-box, a purine-rich DNA sequence (5'-GAGGAA-3') that can act as a lymphoid-specific enhancer. This protein is a transcriptional activator that may be specifically involved in the differentiation or activation of macrophages or B-cells. Also binds RNA and may modulate pre-mRNA splicing.<ref>PMID:8626664</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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/main_output.php?pdb_ID=1pue ConSurf]. | </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/main_output.php?pdb_ID=1pue ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The Ets family of transcription factors, of which there are now about 35 members regulate gene expression during growth and development. They share a conserved domain of around 85 amino acids which binds as a monomer to the DNA sequence 5'-C/AGGAA/T-3'. We have determined the crystal structure of an ETS domain complexed with DNA, at 2.3-A resolution. The domain is similar to alpha + beta (winged) 'helix-turn-helix' proteins and interacts with a ten-base-pair region of duplex DNA which takes up a uniform curve of 8 degrees. The domain contacts the DNA by a novel loop-helix-loop architecture. Four of amino acids that directly interact with the DNA are highly conserved: two arginines from the recognition helix lying in the major groove, one lysine from the 'wing' that binds upstream of the core GGAA sequence, and another lysine, from the 'turn' of the 'helix-turn-helix' motif, which binds downstream and on the opposite strand. | ||
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- | A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS-domain-DNA complex.,Kodandapani R, Pio F, Ni CZ, Piccialli G, Klemsz M, McKercher S, Maki RA, Ely KR Nature. 1996 Apr 4;380(6573):456-60. PMID:8602247<ref>PMID:8602247</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1pue" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Mus musculus]] |
- | [[Category: Ely | + | [[Category: Synthetic construct]] |
- | [[Category: Klemsz | + | [[Category: Ely KR]] |
- | [[Category: Kodandapani | + | [[Category: Klemsz M]] |
- | [[Category: Maki | + | [[Category: Kodandapani R]] |
- | [[Category: McKercher | + | [[Category: Maki RA]] |
- | [[Category: Ni | + | [[Category: McKercher S]] |
- | [[Category: Piccialli | + | [[Category: Ni CZ]] |
- | [[Category: Pio | + | [[Category: Piccialli G]] |
- | + | [[Category: Pio F]] | |
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Current revision
PU.1 ETS DOMAIN-DNA COMPLEX
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Categories: Large Structures | Mus musculus | Synthetic construct | Ely KR | Klemsz M | Kodandapani R | Maki RA | McKercher S | Ni CZ | Piccialli G | Pio F