2lkx - Revision history

OCA at 06:56, 1 May 2024

OCA — Wed, 01 May 2024 06:56:07 GMT

←Older revision		Revision as of 06:56, 1 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2lkx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LKX FirstGlance]. <br>		<table><tr><td colspan='2'>[[2lkx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LKX 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=2lkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkx OCA], [https://pdbe.org/2lkx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lkx RCSB], [https://www.ebi.ac.uk/pdbsum/2lkx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lkx ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkx OCA], [https://pdbe.org/2lkx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lkx RCSB], [https://www.ebi.ac.uk/pdbsum/2lkx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lkx ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 10:		Line 11:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/PITX2_HUMAN PITX2_HUMAN] Controls cell proliferation in a tissue-specific manner and is involved in morphogenesis. During embryonic development, exerts a role in the expansion of muscle progenitors. May play a role in the proper localization of asymmetric organs such as the heart and stomach. Isoform PTX2C is involved in left-right asymmetry the developing embryo (By similarity).		[https://www.uniprot.org/uniprot/PITX2_HUMAN PITX2_HUMAN] Controls cell proliferation in a tissue-specific manner and is involved in morphogenesis. During embryonic development, exerts a role in the expansion of muscle progenitors. May play a role in the proper localization of asymmetric organs such as the heart and stomach. Isoform PTX2C is involved in left-right asymmetry the developing embryo (By similarity).
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	We have determined the solution structure of a complex containing the K50 class homeodomain Pituitary homeobox protein 2 (PITX2) bound to its consensus DNA site (TAATCC). Previous studies have suggested that residue 50 is an important determinant of differential DNA-binding specificity among homeodomains. Although structures of several homeodomain-DNA complexes have been determined, this is the first structure of a native K50 class homeodomain. The only K50 homeodomain structure determined previously is an X-ray crystal structure of an altered specificity mutant, Engrailed Q50K (EnQ50K). Analysis of the NMR structure of the PITX2 homeodomain indicates that the lysine at position 50 makes contacts with two guanines on the antisense strand of the DNA, adjacent to the TAAT core DNA sequence, consistent with the structure of EnQ50K. Our evidence suggests that this side chain may make fluctuating interactions with the DNA, which is complementary to the crystal data for EnQ50K. There are differences in the tertiary structure between the native K50 structure and that of EnQ50K, which may explain differences in affinity and specificity between these proteins. Mutations in the human PITX2 gene are responsible for Rieger syndrome, an autosomal dominant disorder. Analysis of the residues mutated in Rieger syndrome indicates that many of these residues are involved in DNA binding, while others are involved in formation of the hydrophobic core of the protein. Overall, the role of K50 in homeodomain recognition is further clarified, and the results indicate that native K50 homeodomains may exhibit differences from altered specificity mutants.
-
-	Solution structure of the K50 class homeodomain PITX2 bound to DNA and implications for mutations that cause Rieger syndrome.,Chaney BA, Clark-Baldwin K, Dave V, Ma J, Rance M Biochemistry. 2005 May 24;44(20):7497-511. PMID:15895993<ref>PMID:15895993</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2lkx" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 11:05, 15 February 2023

OCA — Wed, 15 Feb 2023 11:05:56 GMT

←Older revision		Revision as of 11:05, 15 February 2023
Line 1:		Line 1:

	==NMR structure of the homeodomain of Pitx2 in complex with a TAATCC DNA binding site==		==NMR structure of the homeodomain of Pitx2 in complex with a TAATCC DNA binding site==
-	<StructureSection load='2lkx' size='340' side='right'caption='[[2lkx~~]], [[NMR_Ensembles_of_Models \| 17 NMR models~~]]' scene=''>	+	<StructureSection load='2lkx' size='340' side='right'caption='[[2lkx]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2lkx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LKX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2lkx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LKX FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PITX3, PTX3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2lkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkx OCA], [https://pdbe.org/2lkx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lkx RCSB], [https://www.ebi.ac.uk/pdbsum/2lkx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lkx 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=2lkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkx OCA], [https://pdbe.org/2lkx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lkx RCSB], [https://www.ebi.ac.uk/pdbsum/2lkx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lkx ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/~~PITX3_HUMAN PITX3_HUMAN~~]~~] Posterior polar cataract~~;~~Cataract-glaucoma~~;~~Familial ocular anterior segment mesenchymal dysgenesis~~. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.	+	[https://www.uniprot.org/uniprot/PITX2_HUMAN PITX2_HUMAN] Peters anomaly;Axenfeld anomaly;Rieger anomaly;Ring dermoid of cornea;Axenfeld-Rieger syndrome. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~PITX3_HUMAN PITX3_HUMAN~~]] Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development. In addition to its importance during development, it also has roles in ~~the long~~-~~term survival~~ and maintenance of the mdDA neurons. Activates NR4A2/NURR1-mediated transcription of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons. Acts by decreasing the interaction of NR4A2/NURR1 with the corepressor NCOR2/SMRT which acts through histone deacetylases (HDACs) to keep promoters of NR4A2/NURR1 target genes in ~~a repressed deacetylated state~~. ~~Essential for the normal lens~~ development ~~and differentiation. Plays~~ a ~~critical~~ role in the ~~maintenance~~ of ~~mitotic activity of lens epithelial cells, fiber cell differentiation and~~ in the ~~control~~ of the ~~temporal~~ and ~~spatial activation of fiber cell-specific crystallins~~. ~~Positively regulates FOXE3 expression and negatively regulates PROX1~~ in the ~~anterior lens epithelium, preventing activation of CDKN1B/P27Kip1 and CDKN1C/P57Kip2 and thus maintains lens epithelial cells in cell cycle~~ (By similarity).	+	[https://www.uniprot.org/uniprot/PITX2_HUMAN PITX2_HUMAN] Controls cell proliferation in a tissue-specific manner and is involved in morphogenesis. During embryonic development, exerts a role in the expansion of muscle progenitors. May play a role in the proper localization of asymmetric organs such as the heart and stomach. Isoform PTX2C is involved in left-right asymmetry the developing embryo (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Baird-Titus~~, J M~~]]	+	[[Category: Baird-Titus JM]]
-	[[Category: Chaney~~, B A~~]]	+	[[Category: Chaney BA]]
-	[[Category: Clark-Baldwin, K]]	+	[[Category: Clark-Baldwin K]]
-	[[Category: Dave, V]]	+	[[Category: Dave V]]
-	[[Category: Doerdelmann, T]]	+	[[Category: Doerdelmann T]]
-	[[Category: Ma, J]]	+	[[Category: Ma J]]
-	~~[[Category: Transcription-dna complex~~]]	+

OCA at 10:12, 12 May 2021

OCA — Wed, 12 May 2021 10:12:40 GMT

←Older revision		Revision as of 10:12, 12 May 2021
Line 1:		Line 1:

	==NMR structure of the homeodomain of Pitx2 in complex with a TAATCC DNA binding site==		==NMR structure of the homeodomain of Pitx2 in complex with a TAATCC DNA binding site==
-	<StructureSection load='2lkx' size='340' side='right' caption='[[2lkx]], [[NMR_Ensembles_of_Models \| 17 NMR models]]' scene=''>	+	<StructureSection load='2lkx' size='340' side='right'caption='[[2lkx]], [[NMR_Ensembles_of_Models \| 17 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2lkx]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2LKX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2lkx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LKX FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PITX3, PTX3 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PITX3, PTX3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2lkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkx OCA], [~~http~~://pdbe.org/2lkx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2lkx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2lkx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2lkx 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=2lkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkx OCA], [https://pdbe.org/2lkx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lkx RCSB], [https://www.ebi.ac.uk/pdbsum/2lkx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lkx ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/PITX3_HUMAN PITX3_HUMAN]] Posterior polar cataract;Cataract-glaucoma;Familial ocular anterior segment mesenchymal dysgenesis. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.	+	[[https://www.uniprot.org/uniprot/PITX3_HUMAN PITX3_HUMAN]] Posterior polar cataract;Cataract-glaucoma;Familial ocular anterior segment mesenchymal dysgenesis. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PITX3_HUMAN PITX3_HUMAN]] Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development. In addition to its importance during development, it also has roles in the long-term survival and maintenance of the mdDA neurons. Activates NR4A2/NURR1-mediated transcription of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons. Acts by decreasing the interaction of NR4A2/NURR1 with the corepressor NCOR2/SMRT which acts through histone deacetylases (HDACs) to keep promoters of NR4A2/NURR1 target genes in a repressed deacetylated state. Essential for the normal lens development and differentiation. Plays a critical role in the maintenance of mitotic activity of lens epithelial cells, fiber cell differentiation and in the control of the temporal and spatial activation of fiber cell-specific crystallins. Positively regulates FOXE3 expression and negatively regulates PROX1 in the anterior lens epithelium, preventing activation of CDKN1B/P27Kip1 and CDKN1C/P57Kip2 and thus maintains lens epithelial cells in cell cycle (By similarity).	+	[[https://www.uniprot.org/uniprot/PITX3_HUMAN PITX3_HUMAN]] Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development. In addition to its importance during development, it also has roles in the long-term survival and maintenance of the mdDA neurons. Activates NR4A2/NURR1-mediated transcription of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons. Acts by decreasing the interaction of NR4A2/NURR1 with the corepressor NCOR2/SMRT which acts through histone deacetylases (HDACs) to keep promoters of NR4A2/NURR1 target genes in a repressed deacetylated state. Essential for the normal lens development and differentiation. Plays a critical role in the maintenance of mitotic activity of lens epithelial cells, fiber cell differentiation and in the control of the temporal and spatial activation of fiber cell-specific crystallins. Positively regulates FOXE3 expression and negatively regulates PROX1 in the anterior lens epithelium, preventing activation of CDKN1B/P27Kip1 and CDKN1C/P57Kip2 and thus maintains lens epithelial cells in cell cycle (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Baird-Titus, J M]]		[[Category: Baird-Titus, J M]]
	[[Category: Chaney, B A]]		[[Category: Chaney, B A]]

OCA at 20:08, 1 August 2018

OCA — Wed, 01 Aug 2018 20:08:23 GMT

←Older revision		Revision as of 20:08, 1 August 2018
Line 1:		Line 1:
		+
	==NMR structure of the homeodomain of Pitx2 in complex with a TAATCC DNA binding site==		==NMR structure of the homeodomain of Pitx2 in complex with a TAATCC DNA binding site==
	<StructureSection load='2lkx' size='340' side='right' caption='[[2lkx]], [[NMR_Ensembles_of_Models \| 17 NMR models]]' scene=''>		<StructureSection load='2lkx' size='340' side='right' caption='[[2lkx]], [[NMR_Ensembles_of_Models \| 17 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[2lkx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LKX FirstGlance]. <br>		<table><tr><td colspan='2'>[[2lkx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LKX FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PITX3, PTX3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PITX3, PTX3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2lkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkx OCA], [http://pdbe.org/2lkx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lkx RCSB], [http://www.ebi.ac.uk/pdbsum/2lkx 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=2lkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkx OCA], [http://pdbe.org/2lkx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lkx RCSB], [http://www.ebi.ac.uk/pdbsum/2lkx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lkx ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 06:33, 11 September 2015

OCA — Fri, 11 Sep 2015 06:33:50 GMT

←Older revision		Revision as of 06:33, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2lkx' size='340' side='right' caption='[[2lkx]], [[NMR_Ensembles_of_Models \| 17 NMR models]]' scene=''>		<StructureSection load='2lkx' size='340' side='right' caption='[[2lkx]], [[NMR_Ensembles_of_Models \| 17 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2lkx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LKX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2lkx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LKX FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PITX3, PTX3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PITX3, PTX3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2lkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lkx RCSB], [http://www.ebi.ac.uk/pdbsum/2lkx 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=2lkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkx OCA], [http://pdbe.org/2lkx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lkx RCSB], [http://www.ebi.ac.uk/pdbsum/2lkx PDBsum]</span></td></tr>
	</table>		</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/PITX3_HUMAN PITX3_HUMAN]] Posterior polar cataract;Cataract-glaucoma;Familial ocular anterior segment mesenchymal dysgenesis. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PITX3_HUMAN PITX3_HUMAN]] Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development. In addition to its importance during development, it also has roles in the long-term survival and maintenance of the mdDA neurons. Activates NR4A2/NURR1-mediated transcription of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons. Acts by decreasing the interaction of NR4A2/NURR1 with the corepressor NCOR2/SMRT which acts through histone deacetylases (HDACs) to keep promoters of NR4A2/NURR1 target genes in a repressed deacetylated state. Essential for the normal lens development and differentiation. Plays a critical role in the maintenance of mitotic activity of lens epithelial cells, fiber cell differentiation and in the control of the temporal and spatial activation of fiber cell-specific crystallins. Positively regulates FOXE3 expression and negatively regulates PROX1 in the anterior lens epithelium, preventing activation of CDKN1B/P27Kip1 and CDKN1C/P57Kip2 and thus maintains lens epithelial cells in cell cycle (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 14:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2lkx" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Baird-Titus, J M]]		[[Category: Baird-Titus, J M]]
	[[Category: Chaney, B A]]		[[Category: Chaney, B A]]

OCA at 22:18, 3 January 2015

OCA — Sat, 03 Jan 2015 22:18:57 GMT

←Older revision		Revision as of 22:18, 3 January 2015
Line 2:		Line 2:
	<StructureSection load='2lkx' size='340' side='right' caption='[[2lkx]], [[NMR_Ensembles_of_Models \| 17 NMR models]]' scene=''>		<StructureSection load='2lkx' size='340' side='right' caption='[[2lkx]], [[NMR_Ensembles_of_Models \| 17 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2lkx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA]. <br>	+	<table><tr><td colspan='2'>[[2lkx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LKX FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PITX3, PTX3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PITX3, PTX3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<tr~~><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class~~='~~plainlinks~~'~~>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=2lkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lkx RCSB], [http://www.ebi.ac.uk/pdbsum/2lkx PDBsum]</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=2lkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lkx RCSB], [http://www.ebi.ac.uk/pdbsum/2lkx PDBsum]</span></td></tr>	+	</table>
-	<table>	+
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 13:		Line 12:
	Solution structure of the K50 class homeodomain PITX2 bound to DNA and implications for mutations that cause Rieger syndrome.,Chaney BA, Clark-Baldwin K, Dave V, Ma J, Rance M Biochemistry. 2005 May 24;44(20):7497-511. PMID:15895993<ref>PMID:15895993</ref>		Solution structure of the K50 class homeodomain PITX2 bound to DNA and implications for mutations that cause Rieger syndrome.,Chaney BA, Clark-Baldwin K, Dave V, Ma J, Rance M Biochemistry. 2005 May 24;44(20):7497-511. PMID:15895993<ref>PMID:15895993</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, a database of the U.S. National Library of Medicine.<br>	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
	== References ==		== References ==
Line 20:		Line 19:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Baird-Titus, J M.]]	+	[[Category: Baird-Titus, J M]]
-	[[Category: Chaney, B A.]]	+	[[Category: Chaney, B A]]
-	[[Category: Clark-Baldwin, K.]]	+	[[Category: Clark-Baldwin, K]]
-	[[Category: Dave, V.]]	+	[[Category: Dave, V]]
-	[[Category: Doerdelmann, T.]]	+	[[Category: Doerdelmann, T]]
-	[[Category: Ma, J.]]	+	[[Category: Ma, J]]
	[[Category: Transcription-dna complex]]		[[Category: Transcription-dna complex]]

OCA at 10:00, 1 May 2014

OCA — Thu, 01 May 2014 10:00:18 GMT

←Older revision		Revision as of 10:00, 1 May 2014
Line 2:		Line 2:
	<StructureSection load='2lkx' size='340' side='right' caption='[[2lkx]], [[NMR_Ensembles_of_Models \| 17 NMR models]]' scene=''>		<StructureSection load='2lkx' size='340' side='right' caption='[[2lkx]], [[NMR_Ensembles_of_Models \| 17 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	[[2lkx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA]. <br>	+	<table><tr><td colspan='2'>[[2lkx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA]. <br>
-	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>	+	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PITX3, PTX3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lkx RCSB], [http://www.ebi.ac.uk/pdbsum/2lkx PDBsum]</span><br>	+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=2lkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lkx RCSB], [http://www.ebi.ac.uk/pdbsum/2lkx PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	We have determined the solution structure of a complex containing the K50 class homeodomain Pituitary homeobox protein 2 (PITX2) bound to its consensus DNA site (TAATCC). Previous studies have suggested that residue 50 is an important determinant of differential DNA-binding specificity among homeodomains. Although structures of several homeodomain-DNA complexes have been determined, this is the first structure of a native K50 class homeodomain. The only K50 homeodomain structure determined previously is an X-ray crystal structure of an altered specificity mutant, Engrailed Q50K (EnQ50K). Analysis of the NMR structure of the PITX2 homeodomain indicates that the lysine at position 50 makes contacts with two guanines on the antisense strand of the DNA, adjacent to the TAAT core DNA sequence, consistent with the structure of EnQ50K. Our evidence suggests that this side chain may make fluctuating interactions with the DNA, which is complementary to the crystal data for EnQ50K. There are differences in the tertiary structure between the native K50 structure and that of EnQ50K, which may explain differences in affinity and specificity between these proteins. Mutations in the human PITX2 gene are responsible for Rieger syndrome, an autosomal dominant disorder. Analysis of the residues mutated in Rieger syndrome indicates that many of these residues are involved in DNA binding, while others are involved in formation of the hydrophobic core of the protein. Overall, the role of K50 in homeodomain recognition is further clarified, and the results indicate that native K50 homeodomains may exhibit differences from altered specificity mutants.		We have determined the solution structure of a complex containing the K50 class homeodomain Pituitary homeobox protein 2 (PITX2) bound to its consensus DNA site (TAATCC). Previous studies have suggested that residue 50 is an important determinant of differential DNA-binding specificity among homeodomains. Although structures of several homeodomain-DNA complexes have been determined, this is the first structure of a native K50 class homeodomain. The only K50 homeodomain structure determined previously is an X-ray crystal structure of an altered specificity mutant, Engrailed Q50K (EnQ50K). Analysis of the NMR structure of the PITX2 homeodomain indicates that the lysine at position 50 makes contacts with two guanines on the antisense strand of the DNA, adjacent to the TAAT core DNA sequence, consistent with the structure of EnQ50K. Our evidence suggests that this side chain may make fluctuating interactions with the DNA, which is complementary to the crystal data for EnQ50K. There are differences in the tertiary structure between the native K50 structure and that of EnQ50K, which may explain differences in affinity and specificity between these proteins. Mutations in the human PITX2 gene are responsible for Rieger syndrome, an autosomal dominant disorder. Analysis of the residues mutated in Rieger syndrome indicates that many of these residues are involved in DNA binding, while others are involved in formation of the hydrophobic core of the protein. Overall, the role of K50 in homeodomain recognition is further clarified, and the results indicate that native K50 homeodomains may exhibit differences from altered specificity mutants.
Line 11:		Line 14:

	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>		From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:25, 30 April 2014

OCA — Wed, 30 Apr 2014 10:25:49 GMT

←Older revision		Revision as of 10:25, 30 April 2014
Line 4:		Line 4:
	[[2lkx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA]. <br>		[[2lkx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA]. <br>
	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>		<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
		+	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lkx RCSB], [http://www.ebi.ac.uk/pdbsum/2lkx PDBsum]</span><br>
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	We have determined the solution structure of a complex containing the K50 class homeodomain Pituitary homeobox protein 2 (PITX2) bound to its consensus DNA site (TAATCC). Previous studies have suggested that residue 50 is an important determinant of differential DNA-binding specificity among homeodomains. Although structures of several homeodomain-DNA complexes have been determined, this is the first structure of a native K50 class homeodomain. The only K50 homeodomain structure determined previously is an X-ray crystal structure of an altered specificity mutant, Engrailed Q50K (EnQ50K). Analysis of the NMR structure of the PITX2 homeodomain indicates that the lysine at position 50 makes contacts with two guanines on the antisense strand of the DNA, adjacent to the TAAT core DNA sequence, consistent with the structure of EnQ50K. Our evidence suggests that this side chain may make fluctuating interactions with the DNA, which is complementary to the crystal data for EnQ50K. There are differences in the tertiary structure between the native K50 structure and that of EnQ50K, which may explain differences in affinity and specificity between these proteins. Mutations in the human PITX2 gene are responsible for Rieger syndrome, an autosomal dominant disorder. Analysis of the residues mutated in Rieger syndrome indicates that many of these residues are involved in DNA binding, while others are involved in formation of the hydrophobic core of the protein. Overall, the role of K50 in homeodomain recognition is further clarified, and the results indicate that native K50 homeodomains may exhibit differences from altered specificity mutants.		We have determined the solution structure of a complex containing the K50 class homeodomain Pituitary homeobox protein 2 (PITX2) bound to its consensus DNA site (TAATCC). Previous studies have suggested that residue 50 is an important determinant of differential DNA-binding specificity among homeodomains. Although structures of several homeodomain-DNA complexes have been determined, this is the first structure of a native K50 class homeodomain. The only K50 homeodomain structure determined previously is an X-ray crystal structure of an altered specificity mutant, Engrailed Q50K (EnQ50K). Analysis of the NMR structure of the PITX2 homeodomain indicates that the lysine at position 50 makes contacts with two guanines on the antisense strand of the DNA, adjacent to the TAAT core DNA sequence, consistent with the structure of EnQ50K. Our evidence suggests that this side chain may make fluctuating interactions with the DNA, which is complementary to the crystal data for EnQ50K. There are differences in the tertiary structure between the native K50 structure and that of EnQ50K, which may explain differences in affinity and specificity between these proteins. Mutations in the human PITX2 gene are responsible for Rieger syndrome, an autosomal dominant disorder. Analysis of the residues mutated in Rieger syndrome indicates that many of these residues are involved in DNA binding, while others are involved in formation of the hydrophobic core of the protein. Overall, the role of K50 in homeodomain recognition is further clarified, and the results indicate that native K50 homeodomains may exhibit differences from altered specificity mutants.

OCA at 08:42, 30 April 2014

OCA — Wed, 30 Apr 2014 08:42:55 GMT

←Older revision		Revision as of 08:42, 30 April 2014
Line 1:		Line 1:
-	[[~~Image:~~2lkx~~.jpg~~\|~~left\|200px~~]]	+	==NMR structure of the homeodomain of Pitx2 in complex with a TAATCC DNA binding site==
		+	<StructureSection load='2lkx' size='340' side='right' caption='[[2lkx]], [[NMR_Ensembles_of_Models \| 17 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	[[2lkx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA]. <br>
		+	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
		+	== Publication Abstract from PubMed ==
		+	We have determined the solution structure of a complex containing the K50 class homeodomain Pituitary homeobox protein 2 (PITX2) bound to its consensus DNA site (TAATCC). Previous studies have suggested that residue 50 is an important determinant of differential DNA-binding specificity among homeodomains. Although structures of several homeodomain-DNA complexes have been determined, this is the first structure of a native K50 class homeodomain. The only K50 homeodomain structure determined previously is an X-ray crystal structure of an altered specificity mutant, Engrailed Q50K (EnQ50K). Analysis of the NMR structure of the PITX2 homeodomain indicates that the lysine at position 50 makes contacts with two guanines on the antisense strand of the DNA, adjacent to the TAAT core DNA sequence, consistent with the structure of EnQ50K. Our evidence suggests that this side chain may make fluctuating interactions with the DNA, which is complementary to the crystal data for EnQ50K. There are differences in the tertiary structure between the native K50 structure and that of EnQ50K, which may explain differences in affinity and specificity between these proteins. Mutations in the human PITX2 gene are responsible for Rieger syndrome, an autosomal dominant disorder. Analysis of the residues mutated in Rieger syndrome indicates that many of these residues are involved in DNA binding, while others are involved in formation of the hydrophobic core of the protein. Overall, the role of K50 in homeodomain recognition is further clarified, and the results indicate that native K50 homeodomains may exhibit differences from altered specificity mutants.

-	~~<!-~~-	+	Solution structure of the K50 class homeodomain PITX2 bound to DNA and implications for mutations that cause Rieger syndrome.,Chaney BA, Clark-Baldwin K, Dave V, Ma J, Rance M Biochemistry. 2005 May 24;44(20):7497-511. PMID:15895993<ref>PMID:15895993</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_2lkx"~~, ~~creates the "Structure Box" on the page~~.	+
-	~~You may change the PDB parameter~~ (~~which sets the PDB file loaded into the applet~~)	+
-	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~	+
-	~~or leave the SCENE parameter empty for the default display~~.	+
-	-->	+
-	~~{{STRUCTURE_2lkx\| PDB=2lkx \| SCENE= }}~~	+

-	~~===NMR structure of the homeodomain of Pitx2 in complex with a TAATCC DNA binding site===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	== References ==
-		+	<references/>
-	~~<!--~~	+	__TOC__
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_15895993}}, adds the Publication Abstract to the page~~	+	</StructureSection>
-	~~(as it appears on PubMed at http:~~/~~/www.pubmed.gov)~~, ~~where 15895993 is the PubMed ID number.~~	+
-	~~-->~~	+
-	~~{{ABSTRACT_PUBMED_15895993}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2lkx]] is~~ a ~~3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes~~ the ~~now removed PDB entry [http://oca~~.~~weizmann~~.~~ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA]~~.	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:015895993<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Baird-Titus, J M.]]		[[Category: Baird-Titus, J M.]]

OCA at 19:14, 2 May 2012

OCA — Wed, 02 May 2012 19:14:28 GMT

←Older revision		Revision as of 19:14, 2 May 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:2lkx.jpg\|left\|200px]]

-	The ~~entry 2lkx~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_2lkx", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_2lkx\| PDB=2lkx \| SCENE= }}

-	~~Authors: Baird-Titus, J.M., Doerdelmann, T., Chaney, B.A., Clark-Baldwin, K., Dave, V., Ma, J.~~	+	===NMR structure of the homeodomain of Pitx2 in complex with a TAATCC DNA binding site===

-	~~Description~~: ~~Chemical shift assignments for~~ the ~~homeodomain of Pitx2 in complex with~~ a ~~TAATCC DNA binding site~~	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_15895993}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 15895993 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_15895993}}
		+
		+	==About this Structure==
		+	[[2lkx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yz8 1yz8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKX OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:015895993</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Baird-Titus, J M.]]
		+	[[Category: Chaney, B A.]]
		+	[[Category: Clark-Baldwin, K.]]
		+	[[Category: Dave, V.]]
		+	[[Category: Doerdelmann, T.]]
		+	[[Category: Ma, J.]]
		+	[[Category: Transcription-dna complex]]