6nog
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Poised-state Dot1L bound to the H2B-Ubiquitinated nucleosome== | |
- | + | <StructureSection load='6nog' size='340' side='right' caption='[[6nog]], [[Resolution|resolution]] 3.90Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[6nog]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NOG FirstGlance]. <br> | |
- | + | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr> | |
- | [[Category: | + | <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=6nog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nog OCA], [http://pdbe.org/6nog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nog RCSB], [http://www.ebi.ac.uk/pdbsum/6nog PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nog ProSAT]</span></td></tr> |
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/DOT1L_HUMAN DOT1L_HUMAN]] Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA. [[http://www.uniprot.org/uniprot/H2A1_XENLA H2A1_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/H4_XENLA H4_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/H32_XENLA H32_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/H2B11_XENLA H2B11_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Histone-lysine N-methyltransferase]] | ||
+ | [[Category: Hoffmann, N A]] | ||
+ | [[Category: Wolberger, C]] | ||
+ | [[Category: Worden, E J]] | ||
+ | [[Category: Methyltransferase]] | ||
+ | [[Category: Nucleosome]] | ||
+ | [[Category: Structural protein-transferase-dna complex]] | ||
+ | [[Category: Ubiquitin]] |
Revision as of 06:56, 21 February 2019
Poised-state Dot1L bound to the H2B-Ubiquitinated nucleosome
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