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4gmb

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==Crystal structure of human WD repeat domain 5 with compound MM-402==
==Crystal structure of human WD repeat domain 5 with compound MM-402==
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<StructureSection load='4gmb' size='340' side='right' caption='[[4gmb]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
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<StructureSection load='4gmb' size='340' side='right'caption='[[4gmb]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4gmb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GMB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GMB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4gmb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GMB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GMB FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=0XQ:(2R)-2,8-DIAMINO-2-METHYLOCTANOIC+ACID'>0XQ</scene>, <scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=ALQ:2-METHYL-PROPIONIC+ACID'>ALQ</scene>, <scene name='pdbligand=PG9:D-PHENYLGLYCINE'>PG9</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.781&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gm3|4gm3]], [[4gm8|4gm8]], [[4gm9|4gm9]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0XQ:(2R)-2,8-DIAMINO-2-METHYLOCTANOIC+ACID'>0XQ</scene>, <scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=ALQ:2-METHYL-PROPIONIC+ACID'>ALQ</scene>, <scene name='pdbligand=PG9:D-PHENYLGLYCINE'>PG9</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">WDR5, BIG3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gmb OCA], [https://pdbe.org/4gmb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gmb RCSB], [https://www.ebi.ac.uk/pdbsum/4gmb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gmb ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gmb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gmb RCSB], [http://www.ebi.ac.uk/pdbsum/4gmb PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/WDR5_HUMAN WDR5_HUMAN]] Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation.<ref>PMID:19556245</ref> <ref>PMID:19103755</ref> <ref>PMID:20018852</ref> <ref>PMID:16600877</ref> <ref>PMID:16829960</ref>
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[https://www.uniprot.org/uniprot/WDR5_HUMAN WDR5_HUMAN] Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation.<ref>PMID:19556245</ref> <ref>PMID:19103755</ref> <ref>PMID:20018852</ref> <ref>PMID:16600877</ref> <ref>PMID:16829960</ref>
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==See Also==
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*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Bernard, D]]
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[[Category: Large Structures]]
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[[Category: Cao, F]]
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[[Category: Bernard D]]
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[[Category: Chen, Y]]
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[[Category: Cao F]]
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[[Category: Dou, Y]]
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[[Category: Chen Y]]
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[[Category: Karatas, H]]
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[[Category: Dou Y]]
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[[Category: Lei, M]]
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[[Category: Karatas H]]
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[[Category: Liu, L]]
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[[Category: Lei M]]
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[[Category: Townsend, E C]]
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[[Category: Liu L]]
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[[Category: Wang, S]]
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[[Category: Townsend EC]]
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[[Category: Histone methyltransferase]]
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[[Category: Wang S]]
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[[Category: Mll1]]
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[[Category: Transcription-transcription inhibitor complex]]
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[[Category: Wd40]]
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Current revision

Crystal structure of human WD repeat domain 5 with compound MM-402

PDB ID 4gmb

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