4rkh
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4rkh]] is a 6 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=4RKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RKH FirstGlance]. <br> | <table><tr><td colspan='2'>[[4rkh]] is a 6 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=4RKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RKH FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4rkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rkh OCA], [https://pdbe.org/4rkh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rkh RCSB], [https://www.ebi.ac.uk/pdbsum/4rkh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rkh 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=4rkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rkh OCA], [https://pdbe.org/4rkh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rkh RCSB], [https://www.ebi.ac.uk/pdbsum/4rkh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rkh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/MSL2_DROME MSL2_DROME] The Msl proteins are essential for elevating transcription of the single X chromosome in the male (X chromosome dosage compensation). Msl-2 is required for translation and/or stability of msl-1 in males. In complex with msl-1, acts as an E3 ubiquitin ligase that promotes ubiquitination of histone H2B.<ref>PMID:21726816</ref> <ref>PMID:7588059</ref> <ref>PMID:7781064</ref> <ref>PMID:7796814</ref> | [https://www.uniprot.org/uniprot/MSL2_DROME MSL2_DROME] The Msl proteins are essential for elevating transcription of the single X chromosome in the male (X chromosome dosage compensation). Msl-2 is required for translation and/or stability of msl-1 in males. In complex with msl-1, acts as an E3 ubiquitin ligase that promotes ubiquitination of histone H2B.<ref>PMID:21726816</ref> <ref>PMID:7588059</ref> <ref>PMID:7781064</ref> <ref>PMID:7796814</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The male-specific lethal dosage compensation complex (MSL-DCC) selectively assembles on the X chromosome in Drosophila males and activates gene transcription by twofold through histone acetylation. An MSL recognition element (MRE) sequence motif nucleates the initial MSL association, but how it is recognized remains unknown. Here, we identified the CXC domain of MSL2 specifically recognizing the MRE motif and determined its crystal structure bound to specific and nonspecific DNAs. The CXC domain primarily contacts one strand of DNA duplex and employs a single arginine to directly read out dinucleotide sequences from the minor groove. The arginine is flexible when bound to nonspecific sequences. The core region of the MRE motif harbors two binding sites on opposite strands that can cooperatively recruit a CXC dimer. Specific DNA-binding mutants of MSL2 are impaired in MRE binding and X chromosome localization in vivo. Our results reveal multiple dynamic DNA-binding modes of the CXC domain that target the MSL-DCC to X chromosomes. | ||
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| - | Structural basis of X chromosome DNA recognition by the MSL2 CXC domain during Drosophila dosage compensation.,Zheng S, Villa R, Wang J, Feng Y, Wang J, Becker PB, Ye K Genes Dev. 2014 Dec 1;28(23):2652-62. doi: 10.1101/gad.250936.114. PMID:25452275<ref>PMID:25452275</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4rkh" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
Structure of the MSL2 CXC domain bound with a specific MRE sequence
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