1kw4
From Proteopedia
(Difference between revisions)
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<StructureSection load='1kw4' size='340' side='right'caption='[[1kw4]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='1kw4' size='340' side='right'caption='[[1kw4]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1kw4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1kw4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KW4 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">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1kw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kw4 OCA], [https://pdbe.org/1kw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kw4 RCSB], [https://www.ebi.ac.uk/pdbsum/1kw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kw4 ProSAT]</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=1kw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kw4 OCA], [https://pdbe.org/1kw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kw4 RCSB], [https://www.ebi.ac.uk/pdbsum/1kw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kw4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/PHP_DROME PHP_DROME] Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. Component of the PcG multiprotein PRC1 complex, a complex that acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-118', rendering chromatin heritably changed in its expressibility. Plays a role in regulating the expression of other pair-rule genes such as eve, ftz, and H.<ref>PMID:1346609</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=1kw4 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=1kw4 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The polycomb group (PcG) proteins are important in the maintenance of stable repression patterns during development. Several PcG members contain a protein protein interaction module called a SAM domain (also known as SPM, PNT and HLH). Here we report the high-resolution structure of the SAM domain of polyhomeotic (Ph). Ph-SAM forms a helical polymer structure, providing a likely mechanism for the extension of PcG complexes. The structure of the polymer resembles that formed by the SAM domain of another transcriptional repressor, TEL. The formation of these polymer structures by SAM domains in two divergent repressors suggests a conserved mode of repression involving a higher order chromatin structure. | ||
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| - | The SAM domain of polyhomeotic forms a helical polymer.,Kim CA, Gingery M, Pilpa RM, Bowie JU Nat Struct Biol. 2002 Jun;9(6):453-7. PMID:11992127<ref>PMID:11992127</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1kw4" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Drosophila melanogaster]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Bowie | + | [[Category: Bowie JU]] |
| - | [[Category: Gingery | + | [[Category: Gingery M]] |
| - | [[Category: Kim | + | [[Category: Kim CA]] |
| - | [[Category: Pilpa | + | [[Category: M Pilpa R]] |
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Revision as of 08:04, 3 April 2024
Polyhomeotic SAM domain structure
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