4pzi - Revision history

OCA at 12:43, 1 March 2024

OCA — Fri, 01 Mar 2024 12:43:35 GMT

←Older revision		Revision as of 12:43, 1 March 2024
Line 1:		Line 1:

	==Zinc finger region of MLL2 in complex with CpG DNA==		==Zinc finger region of MLL2 in complex with CpG DNA==
-	<StructureSection load='4pzi' size='340' side='right'caption='[[4pzi]]' scene=''>	+	<StructureSection load='4pzi' size='340' side='right'caption='[[4pzi]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PZI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4pzi]] is a 3 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=4PZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PZI FirstGlance]. <br>
-	</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=4pzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzi OCA], [https://pdbe.org/4pzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pzi RCSB], [https://www.ebi.ac.uk/pdbsum/4pzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pzi ProSAT]</span></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]] 2.15Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <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=4pzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzi OCA], [https://pdbe.org/4pzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pzi RCSB], [https://www.ebi.ac.uk/pdbsum/4pzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pzi ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/KMT2B_HUMAN KMT2B_HUMAN] Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in beta-globin locus transcription regulation by being recruited by NFE2. Plays an important role in controlling bulk H3K4me during oocyte growth and preimplantation development. Required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that preceeds resumption of meiosis, oocyte survival and normal zygotic genome activation.<ref>PMID:17707229</ref>

	==See Also==		==See Also==
	*[[Histone methyltransferase 3D structures\|Histone methyltransferase 3D structures]]		*[[Histone methyltransferase 3D structures\|Histone methyltransferase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Arrowsmith CH]]		[[Category: Arrowsmith CH]]

OCA at 10:53, 31 August 2022

OCA — Wed, 31 Aug 2022 10:53:22 GMT

←Older revision		Revision as of 10:53, 31 August 2022
Line 1:		Line 1:

	==Zinc finger region of MLL2 in complex with CpG DNA==		==Zinc finger region of MLL2 in complex with CpG DNA==
-	<StructureSection load='4pzi' size='340' side='right'caption='[[4pzi]]~~, [[Resolution\|resolution]] 2.15Å~~' scene=''>	+	<StructureSection load='4pzi' size='340' side='right'caption='[[4pzi]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>~~[[4pzi]] is a 3 chain structure.~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PZI FirstGlance]. <br>	+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PZI FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</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=4pzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzi OCA], [https://pdbe.org/4pzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pzi RCSB], [https://www.ebi.ac.uk/pdbsum/4pzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pzi ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </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=4pzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzi OCA], [https://pdbe.org/4pzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pzi RCSB], [https://www.ebi.ac.uk/pdbsum/4pzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pzi ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Function ==
-	[[https://www.uniprot.org/uniprot/KMT2B_HUMAN KMT2B_HUMAN]] Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in beta-globin locus transcription regulation by being recruited by NFE2. Plays an important role in controlling bulk H3K4me during oocyte growth and preimplantation development. Required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that preceeds resumption of meiosis, oocyte survival and normal zygotic genome activation.<ref>PMID:17707229</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The CXXC domain, first identified as the reader of unmodified CpG dinucleotide, plays important roles in epigenetic regulation by targeting various activities to CpG islands. Here we systematically measured and compared the DNA-binding selectivities of all known human CXXC domains by different binding assays, and complemented the existing function-based classification of human CXXC domains with a classification based on their DNA selectivities. Through a series of crystal structures of CXXC domains with DNA ligands, we unravel the molecular mechanisms of how these CXXC domains, including single CXXC domains and tandem CXXC-PHD domains, recognize distinct DNA ligands, which further supports our classification of human CXXC domains and also provides insights into selective recruitment of chromatin modifiers to their respective targets via CXXC domains recognizing different genomic DNA sequences. Our study facilitates the understanding of the relationship between the DNA-binding specificities of the CXXC proteins and their biological functions.
-
-	DNA Sequence Recognition of Human CXXC Domains and Their Structural Determinants.,Xu C, Liu K, Lei M, Yang A, Li Y, Hughes TR, Min J Structure. 2017 Dec 16. pii: S0969-2126(17)30396-9. doi:, 10.1016/j.str.2017.11.022. PMID:29276034<ref>PMID:29276034</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4pzi" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Histone methyltransferase 3D structures\|Histone methyltransferase 3D structures]]		*[[Histone methyltransferase 3D structures\|Histone methyltransferase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Histone-lysine N-methyltransferase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Arrowsmith~~, C H~~]]	+	[[Category: Arrowsmith CH]]
-	[[Category: Bountra, C]]	+	[[Category: Bountra C]]
-	[[Category: Chao, X]]	+	[[Category: Chao X]]
-	[[Category: Dong, A]]	+	[[Category: Dong A]]
-	[[Category: Edwards~~, A M~~]]	+	[[Category: Edwards AM]]
-	[[Category: Liu, K]]	+	[[Category: Liu K]]
-	[[Category: Min, J]]	+	[[Category: Min J]]
-	~~[[Category: Structural genomic~~]]	+	[[Category: Tempel W]]
-	[[Category: Tempel, W]]	+	[[Category: Weigelt J]]
-	[[Category: Weigelt, J]]	+
-	~~[[Category: Dna-binding]]~~	+
-	~~[[Category: Sgc]]~~	+
-	~~[[Category: Transcription-dna complex]]~~	+
-	~~[[Category: Zinc finger~~]]	+

OCA at 05:06, 25 August 2022

OCA — Thu, 25 Aug 2022 05:06:21 GMT

←Older revision		Revision as of 05:06, 25 August 2022
Line 1:		Line 1:

	==Zinc finger region of MLL2 in complex with CpG DNA==		==Zinc finger region of MLL2 in complex with CpG DNA==
-	<StructureSection load='4pzi' size='340' side='right' caption='[[4pzi]], [[Resolution\|resolution]] 2.15Å' scene=''>	+	<StructureSection load='4pzi' size='340' side='right'caption='[[4pzi]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4pzi]] is a 3 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=4PZI OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4PZI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4pzi]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PZI FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <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" id="ligandDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KMT2B, HRX2, KIAA0304, MLL2, MLL4, TRX2, WBP7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></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>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzi OCA], [https://pdbe.org/4pzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pzi RCSB], [https://www.ebi.ac.uk/pdbsum/4pzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pzi 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=4pzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzi OCA], [~~http~~://pdbe.org/4pzi PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4pzi RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4pzi PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4pzi ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/KMT2B_HUMAN KMT2B_HUMAN]] Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in beta-globin locus transcription regulation by being recruited by NFE2. Plays an important role in controlling bulk H3K4me during oocyte growth and preimplantation development. Required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that preceeds resumption of meiosis, oocyte survival and normal zygotic genome activation.<ref>PMID:17707229</ref>	+	[[https://www.uniprot.org/uniprot/KMT2B_HUMAN KMT2B_HUMAN]] Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in beta-globin locus transcription regulation by being recruited by NFE2. Plays an important role in controlling bulk H3K4me during oocyte growth and preimplantation development. Required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that preceeds resumption of meiosis, oocyte survival and normal zygotic genome activation.<ref>PMID:17707229</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 4pzi" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4pzi" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Histone methyltransferase 3D structures\|Histone methyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 25:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
-	[[Category: ~~Human~~]]	+	[[Category: Large Structures]]
	[[Category: Arrowsmith, C H]]		[[Category: Arrowsmith, C H]]
	[[Category: Bountra, C]]		[[Category: Bountra, C]]

OCA at 05:54, 3 January 2018

OCA — Wed, 03 Jan 2018 05:54:56 GMT

←Older revision		Revision as of 05:54, 3 January 2018
Line 3:		Line 3:
	<StructureSection load='4pzi' size='340' side='right' caption='[[4pzi]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='4pzi' size='340' side='right' caption='[[4pzi]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4pzi]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PZI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4pzi]] is a 3 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=4PZI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PZI FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <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=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KMT2B, HRX2, KIAA0304, MLL2, MLL4, TRX2, WBP7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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>		<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>
	<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=4pzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzi OCA], [http://pdbe.org/4pzi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pzi RCSB], [http://www.ebi.ac.uk/pdbsum/4pzi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pzi 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=4pzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzi OCA], [http://pdbe.org/4pzi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pzi RCSB], [http://www.ebi.ac.uk/pdbsum/4pzi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pzi ProSAT]</span></td></tr>
Line 10:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/KMT2B_HUMAN KMT2B_HUMAN]] Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in beta-globin locus transcription regulation by being recruited by NFE2. Plays an important role in controlling bulk H3K4me during oocyte growth and preimplantation development. Required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that preceeds resumption of meiosis, oocyte survival and normal zygotic genome activation.<ref>PMID:17707229</ref>		[[http://www.uniprot.org/uniprot/KMT2B_HUMAN KMT2B_HUMAN]] Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in beta-globin locus transcription regulation by being recruited by NFE2. Plays an important role in controlling bulk H3K4me during oocyte growth and preimplantation development. Required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that preceeds resumption of meiosis, oocyte survival and normal zygotic genome activation.<ref>PMID:17707229</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The CXXC domain, first identified as the reader of unmodified CpG dinucleotide, plays important roles in epigenetic regulation by targeting various activities to CpG islands. Here we systematically measured and compared the DNA-binding selectivities of all known human CXXC domains by different binding assays, and complemented the existing function-based classification of human CXXC domains with a classification based on their DNA selectivities. Through a series of crystal structures of CXXC domains with DNA ligands, we unravel the molecular mechanisms of how these CXXC domains, including single CXXC domains and tandem CXXC-PHD domains, recognize distinct DNA ligands, which further supports our classification of human CXXC domains and also provides insights into selective recruitment of chromatin modifiers to their respective targets via CXXC domains recognizing different genomic DNA sequences. Our study facilitates the understanding of the relationship between the DNA-binding specificities of the CXXC proteins and their biological functions.

-	==~~See Also==~~	+	DNA Sequence Recognition of Human CXXC Domains and Their Structural Determinants.,Xu C, Liu K, Lei M, Yang A, Li Y, Hughes TR, Min J Structure. 2017 Dec 16. pii: S0969-2126(17)30396-9. doi:, 10.1016/j.str.2017.11.022. PMID:29276034<ref>PMID:29276034</ref>
-	*[[Histone methyltransferase\|Histone methyltransferase]]	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4pzi" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 18:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
		+	[[Category: Human]]
	[[Category: Arrowsmith, C H]]		[[Category: Arrowsmith, C H]]
	[[Category: Bountra, C]]		[[Category: Bountra, C]]

OCA at 20:06, 5 August 2016

OCA — Fri, 05 Aug 2016 20:06:18 GMT

←Older revision		Revision as of 20:06, 5 August 2016
Line 1:		Line 1:
		+
	==Zinc finger region of MLL2 in complex with CpG DNA==		==Zinc finger region of MLL2 in complex with CpG DNA==
	<StructureSection load='4pzi' size='340' side='right' caption='[[4pzi]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='4pzi' size='340' side='right' caption='[[4pzi]], [[Resolution\|resolution]] 2.15Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <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=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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>		<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>
-	<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=4pzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pzi RCSB], [http://www.ebi.ac.uk/pdbsum/4pzi PDBsum]</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=4pzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzi OCA], [http://pdbe.org/4pzi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pzi RCSB], [http://www.ebi.ac.uk/pdbsum/4pzi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pzi ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 05:28, 25 December 2014

OCA — Thu, 25 Dec 2014 05:28:22 GMT

←Older revision		Revision as of 05:28, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4pzi]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PZI FirstGlance]. <br>		<table><tr><td colspan='2'>[[4pzi]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PZI FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><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>	+	<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>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pzi RCSB], [http://www.ebi.ac.uk/pdbsum/4pzi PDBsum]</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=4pzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pzi RCSB], [http://www.ebi.ac.uk/pdbsum/4pzi PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/KMT2B_HUMAN KMT2B_HUMAN]] Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in beta-globin locus transcription regulation by being recruited by NFE2. Plays an important role in controlling bulk H3K4me during oocyte growth and preimplantation development. Required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that preceeds resumption of meiosis, oocyte survival and normal zygotic genome activation.<ref>PMID:17707229</ref>
		+
		+	==See Also==
		+	*[[Histone methyltransferase\|Histone methyltransferase]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
-	[[Category: Arrowsmith, C H.]]	+	[[Category: Arrowsmith, C H]]
-	[[Category: Bountra, C.]]	+	[[Category: Bountra, C]]
-	[[Category: Chao, X.]]	+	[[Category: Chao, X]]
-	[[Category: Dong, A.]]	+	[[Category: Dong, A]]
-	[[Category: Edwards, A M.]]	+	[[Category: Edwards, A M]]
-	[[Category: Liu, K.]]	+	[[Category: Liu, K]]
-	[[Category: Min, J.]]	+	[[Category: Min, J]]
-	[[Category: ~~SGC,~~ Structural ~~Genomics Consortium.~~]]	+	[[Category: Structural genomic]]
-	[[Category: Tempel, W.]]	+	[[Category: Tempel, W]]
-	[[Category: Weigelt, J.]]	+	[[Category: Weigelt, J]]
	[[Category: Dna-binding]]		[[Category: Dna-binding]]
	[[Category: Sgc]]		[[Category: Sgc]]
-	[[Category: Structural genomic]]
-	[[Category: Structural genomics consortium]]
	[[Category: Transcription-dna complex]]		[[Category: Transcription-dna complex]]
	[[Category: Zinc finger]]		[[Category: Zinc finger]]

OCA at 05:14, 4 June 2014

OCA — Wed, 04 Jun 2014 05:14:56 GMT

←Older revision		Revision as of 05:14, 4 June 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Zinc finger region of MLL2 in complex with CpG DNA==
-		+	<StructureSection load='4pzi' size='340' side='right' caption='[[4pzi]], [[Resolution\|resolution]] 2.15Å' scene=''>
-	~~The entry~~ 4pzi is ~~ON HOLD until Jun 01 2015~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4pzi]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PZI FirstGlance]. <br>
-	~~Authors~~: ~~Chao~~, X., ~~Tempel, W~~., ~~Liu, K~~., ~~Dong, A~~., Bountra, C., ~~Weigelt, J~~., ~~Arrowsmith, C.H~~., Edwards, A.M., Min, J., Structural Genomics Consortium ~~(SGC)~~	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
-		+	<tr><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>
-	~~Description~~: Zinc finger ~~region of MLL2 in complex with CpG DNA~~	+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pzi RCSB], [http://www.ebi.ac.uk/pdbsum/4pzi PDBsum]</span></td></tr>
		+	<table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Histone-lysine N-methyltransferase]]
		+	[[Category: Arrowsmith, C H.]]
		+	[[Category: Bountra, C.]]
		+	[[Category: Chao, X.]]
		+	[[Category: Dong, A.]]
		+	[[Category: Edwards, A M.]]
		+	[[Category: Liu, K.]]
		+	[[Category: Min, J.]]
		+	[[Category: SGC, Structural Genomics Consortium.]]
		+	[[Category: Tempel, W.]]
		+	[[Category: Weigelt, J.]]
		+	[[Category: Dna-binding]]
		+	[[Category: Sgc]]
		+	[[Category: Structural genomic]]
		+	[[Category: Structural genomics consortium]]
		+	[[Category: Transcription-dna complex]]
		+	[[Category: Zinc finger]]

OCA at 09:09, 16 April 2014

OCA — Wed, 16 Apr 2014 09:09:00 GMT

←Older revision		Revision as of 09:09, 16 April 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4pzi is ON HOLD	+	The entry 4pzi is ON HOLD until Jun 01 2015

-	Authors: Chao, X., Tempel, W., Dong, A., Bountra, C., Weigelt, J., Arrowsmith, C.H., Edwards, A.M., Min, J., Structural Genomics Consortium (SGC)	+	Authors: Chao, X., Tempel, W., Liu, K., Dong, A., Bountra, C., Weigelt, J., Arrowsmith, C.H., Edwards, A.M., Min, J., Structural Genomics Consortium (SGC)

	Description: Zinc finger region of MLL2 in complex with CpG DNA		Description: Zinc finger region of MLL2 in complex with CpG DNA

OCA: Protected "4pzi" [edit=sysop:move=sysop]

OCA — Wed, 09 Apr 2014 05:59:04 GMT

Protected "4pzi" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:59, 9 April 2014

OCA: New page: '''Unreleased structure''' The entry 4pzi is ON HOLD Authors: Chao, X., Tempel, W., Dong, A., Bountra, C., Weigelt, J., Arrowsmith, C.H., Edwards, A.M., Min, J., Structural Genomics Con...

OCA — Wed, 09 Apr 2014 05:59:03 GMT

New page: '''Unreleased structure''' The entry 4pzi is ON HOLD Authors: Chao, X., Tempel, W., Dong, A., Bountra, C., Weigelt, J., Arrowsmith, C.H., Edwards, A.M., Min, J., Structural Genomics Con...

New page

'''Unreleased structure'''

The entry 4pzi is ON HOLD

Authors: Chao, X., Tempel, W., Dong, A., Bountra, C., Weigelt, J., Arrowsmith, C.H., Edwards, A.M., Min, J., Structural Genomics Consortium (SGC)

Description: Zinc finger region of MLL2 in complex with CpG DNA