5yc3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
==Crystal structure of AL3 PHD finger bound to H3K4me2==
==Crystal structure of AL3 PHD finger bound to H3K4me2==
-
<StructureSection load='5yc3' size='340' side='right' caption='[[5yc3]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+
<StructureSection load='5yc3' size='340' side='right'caption='[[5yc3]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5yc3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YC3 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5yc3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YC3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AL3, At3g42790, T21C14_10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
<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=5yc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yc3 OCA], [http://pdbe.org/5yc3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yc3 RCSB], [http://www.ebi.ac.uk/pdbsum/5yc3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yc3 ProSAT]</span></td></tr>
<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=5yc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yc3 OCA], [http://pdbe.org/5yc3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yc3 RCSB], [http://www.ebi.ac.uk/pdbsum/5yc3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yc3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ALFL3_ARATH ALFL3_ARATH]] Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
[[http://www.uniprot.org/uniprot/ALFL3_ARATH ALFL3_ARATH]] Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Histone post-translational modifications (PTMs) and their recognition by histone readers exert crucial functions in eukaryotes. Despite extensive studies, conservation and diversity of histone PTM regulation between animals and plants remain less explored because of a lack of systematic knowledge of histone readers in plants. Based on a high-throughput surface plasmon resonance imaging (SPRi) platform, we report the lab-on-chip profiling of interactions between 204 putative reader domains and 11 types of histone peptides in Arabidopsis thaliana. Eleven reader hits were then chosen for histone combinatorial readout pattern profiling. Systematic analysis of histone PTM recognition in Arabidopsis thaliana reveals that plant and human histone readers share conservation in domain types and recognition mechanisms. The differences in particular histone mark recognition by transcription regulator EML1 and DNA damage repair factor MSH6 indicate plant-specific histone PTMs function in Arabidopsis thaliana acquired during evolution.
 +
 +
Systematic Profiling of Histone Readers in Arabidopsis thaliana.,Zhao S, Zhang B, Yang M, Zhu J, Li H Cell Rep. 2018 Jan 23;22(4):1090-1102. doi: 10.1016/j.celrep.2017.12.099. Epub, 2018 Jan 28. PMID:29386129<ref>PMID:29386129</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 5yc3" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Arath]]
 +
[[Category: Large Structures]]
[[Category: Li, H]]
[[Category: Li, H]]
[[Category: Zhang, B]]
[[Category: Zhang, B]]

Revision as of 12:42, 25 December 2019

Crystal structure of AL3 PHD finger bound to H3K4me2

PDB ID 5yc3

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5yc3"
Personal tools