1pk3

<table><tr><td colspan='2'>[[1pk3]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PK3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1PK3 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pk1|1pk1]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Scm ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1pk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pk3 OCA], [http://pdbe.org/1pk3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pk3 RCSB], [http://www.ebi.ac.uk/pdbsum/1pk3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pk3 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/SCM_DROME SCM_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. They probably act via the methylation of histones, rendering chromatin heritably changed in its expressibility.<ref>PMID:15280237</ref> [UniProtKB:Q9W3C1]

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== Publication Abstract from PubMed ==

The polycomb group proteins are required for the stable maintenance of gene repression patterns established during development. They function as part of large multiprotein complexes created via a multitude of protein-protein interaction domains. Here we examine the interaction between the SAM domains of the polycomb group proteins polyhomeotic (Ph) and Sex-comb-on-midleg (Scm). Previously we showed that Ph-SAM polymerizes as a helical structure. We find that Scm-SAM also polymerizes, and a crystal structure reveals an architecture similar to the Ph-SAM polymer. These results suggest that Ph-SAM and Scm-SAM form a copolymer. Binding affinity measurements between Scm-SAM and Ph-SAM subunits in different orientations indicate a preference for the formation of a single junction copolymer. To provide a model of the copolymer, we determined the structure of the Ph-SAM/Scm-SAM junction. Similar binding modes are observed in both homo- and heterocomplex formation with minimal change in helix axis direction at the polymer joint. The copolymer model suggests that polymeric Scm complexes could extend beyond the local domains of polymeric Ph complexes on chromatin, possibly playing a role in long range repression.

Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer.,Kim CA, Sawaya MR, Cascio D, Kim W, Bowie JU J Biol Chem. 2005 Jul 29;280(30):27769-75. Epub 2005 May 19. PMID:15905166<ref>PMID:15905166</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1pk3" style="background-color:#fffaf0;"></div>

[[Category: Drome]]

[[Category: Bowie, J U]]

[[Category: Cascio, D]]

[[Category: Kim, C A]]

[[Category: Kim, W]]

[[Category: Sawaya, M R]]

[[Category: Transcriptional repression]]