2vxd - Revision history

OCA at 07:34, 25 June 2021

OCA — Fri, 25 Jun 2021 07:34:48 GMT

←Older revision		Revision as of 07:34, 25 June 2021
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	<StructureSection load='2vxd' size='340' side='right'caption='[[2vxd]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2vxd' size='340' side='right'caption='[[2vxd]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vxd]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2VXD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vxd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VXD FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=2vxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxd OCA], [~~http~~://pdbe.org/2vxd PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2vxd RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2vxd PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2vxd ProSAT]</span></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=2vxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxd OCA], [https://pdbe.org/2vxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vxd RCSB], [https://www.ebi.ac.uk/pdbsum/2vxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vxd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/NPM_HUMAN NPM_HUMAN]] Note=A chromosomal aberration involving NPM1 is found in a form of non-Hodgkin lymphoma. Translocation t(2;5)(p23;q35) with ALK. The resulting chimeric NPM1-ALK protein homodimerize and the kinase becomes constitutively activated. Note=A chromosomal aberration involving NPM1 is found in a form of acute promyelocytic leukemia. Translocation t(5;17)(q32;q11) with RARA. Note=A chromosomal aberration involving NPM1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with MLF1. Note=Defects in NPM1 are associated with acute myelogenous leukemia (AML). Mutations in exon 12 affecting the C-terminus of the protein are associated with an aberrant cytoplasmic location.	+	[[https://www.uniprot.org/uniprot/NPM_HUMAN NPM_HUMAN]] Note=A chromosomal aberration involving NPM1 is found in a form of non-Hodgkin lymphoma. Translocation t(2;5)(p23;q35) with ALK. The resulting chimeric NPM1-ALK protein homodimerize and the kinase becomes constitutively activated. Note=A chromosomal aberration involving NPM1 is found in a form of acute promyelocytic leukemia. Translocation t(5;17)(q32;q11) with RARA. Note=A chromosomal aberration involving NPM1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with MLF1. Note=Defects in NPM1 are associated with acute myelogenous leukemia (AML). Mutations in exon 12 affecting the C-terminus of the protein are associated with an aberrant cytoplasmic location.
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/NPM_HUMAN NPM_HUMAN]] Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication.<ref>PMID:16107701</ref> <ref>PMID:17015463</ref> <ref>PMID:18809582</ref> <ref>PMID:19188445</ref> <ref>PMID:20352051</ref> <ref>PMID:21084279</ref> <ref>PMID:22002061</ref>	+	[[https://www.uniprot.org/uniprot/NPM_HUMAN NPM_HUMAN]] Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication.<ref>PMID:16107701</ref> <ref>PMID:17015463</ref> <ref>PMID:18809582</ref> <ref>PMID:19188445</ref> <ref>PMID:20352051</ref> <ref>PMID:21084279</ref> <ref>PMID:22002061</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 08:39, 25 June 2020

OCA — Thu, 25 Jun 2020 08:39:05 GMT

←Older revision		Revision as of 08:39, 25 June 2020
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	==The structure of the C-terminal domain of Nucleophosmin==		==The structure of the C-terminal domain of Nucleophosmin==
-	<StructureSection load='2vxd' size='340' side='right' caption='[[2vxd]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='2vxd' size='340' side='right'caption='[[2vxd]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vxd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXD OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2VXD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vxd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VXD FirstGlance]. <br>
-	</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=2vxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxd OCA], [http://pdbe.org/2vxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vxd RCSB], [http://www.ebi.ac.uk/pdbsum/2vxd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vxd ProSAT]</span></td></tr>	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2vxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxd OCA], [http://pdbe.org/2vxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vxd RCSB], [http://www.ebi.ac.uk/pdbsum/2vxd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vxd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Bycroft, M]]		[[Category: Bycroft, M]]
	[[Category: Grummitt, C G]]		[[Category: Grummitt, C G]]

OCA at 20:57, 19 September 2018

OCA — Wed, 19 Sep 2018 20:57:36 GMT

←Older revision		Revision as of 20:57, 19 September 2018
Line 1:		Line 1:
		+
	==The structure of the C-terminal domain of Nucleophosmin==		==The structure of the C-terminal domain of Nucleophosmin==
	<StructureSection load='2vxd' size='340' side='right' caption='[[2vxd]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2vxd' size='340' side='right' caption='[[2vxd]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vxd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VXD FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vxd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VXD FirstGlance]. <br>
-	</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=2vxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxd OCA], [http://pdbe.org/2vxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vxd RCSB], [http://www.ebi.ac.uk/pdbsum/2vxd PDBsum]</span></td></tr>	+	</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=2vxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxd OCA], [http://pdbe.org/2vxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vxd RCSB], [http://www.ebi.ac.uk/pdbsum/2vxd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vxd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vx/2vxd_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vx/2vxd_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 35:		Line 36:
	[[Category: Bycroft, M]]		[[Category: Bycroft, M]]
	[[Category: Grummitt, C G]]		[[Category: Grummitt, C G]]
		+	[[Category: Acetylation]]
		+	[[Category: Alternative splicing]]
	[[Category: Aml]]		[[Category: Aml]]
		+	[[Category: Chromosomal rearrangement]]
	[[Category: Nuclear protein]]		[[Category: Nuclear protein]]
	[[Category: Nucleolus]]		[[Category: Nucleolus]]

OCA at 06:13, 9 February 2016

OCA — Tue, 09 Feb 2016 06:13:26 GMT

←Older revision		Revision as of 06:13, 9 February 2016
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	<StructureSection load='2vxd' size='340' side='right' caption='[[2vxd]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2vxd' size='340' side='right' caption='[[2vxd]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vxd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VXD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vxd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VXD FirstGlance]. <br>
-	</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=2vxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vxd RCSB], [http://www.ebi.ac.uk/pdbsum/2vxd PDBsum]</span></td></tr>	+	</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=2vxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxd OCA], [http://pdbe.org/2vxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vxd RCSB], [http://www.ebi.ac.uk/pdbsum/2vxd PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 17:		Line 17:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vxd ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	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 2vxd" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Bycroft, M]]		[[Category: Bycroft, M]]
	[[Category: Grummitt, C G]]		[[Category: Grummitt, C G]]

OCA at 13:44, 19 January 2015

OCA — Mon, 19 Jan 2015 13:44:48 GMT

←Older revision		Revision as of 13:44, 19 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vxd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VXD FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vxd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VXD FirstGlance]. <br>
-	</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=2vxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vxd RCSB], [http://www.ebi.ac.uk/pdbsum/2vxd PDBsum]</span></td></tr>	+	</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=2vxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vxd RCSB], [http://www.ebi.ac.uk/pdbsum/2vxd PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/NPM_HUMAN NPM_HUMAN]] Note=A chromosomal aberration involving NPM1 is found in a form of non-Hodgkin lymphoma. Translocation t(2;5)(p23;q35) with ALK. The resulting chimeric NPM1-ALK protein homodimerize and the kinase becomes constitutively activated. Note=A chromosomal aberration involving NPM1 is found in a form of acute promyelocytic leukemia. Translocation t(5;17)(q32;q11) with RARA. Note=A chromosomal aberration involving NPM1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with MLF1. Note=Defects in NPM1 are associated with acute myelogenous leukemia (AML). Mutations in exon 12 affecting the C-terminus of the protein are associated with an aberrant cytoplasmic location.		[[http://www.uniprot.org/uniprot/NPM_HUMAN NPM_HUMAN]] Note=A chromosomal aberration involving NPM1 is found in a form of non-Hodgkin lymphoma. Translocation t(2;5)(p23;q35) with ALK. The resulting chimeric NPM1-ALK protein homodimerize and the kinase becomes constitutively activated. Note=A chromosomal aberration involving NPM1 is found in a form of acute promyelocytic leukemia. Translocation t(5;17)(q32;q11) with RARA. Note=A chromosomal aberration involving NPM1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with MLF1. Note=Defects in NPM1 are associated with acute myelogenous leukemia (AML). Mutations in exon 12 affecting the C-terminus of the protein are associated with an aberrant cytoplasmic location.
Line 32:		Line 32:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Bycroft, M.]]	+	[[Category: Bycroft, M]]
-	[[Category: Grummitt, C G.]]	+	[[Category: Grummitt, C G]]
	[[Category: Aml]]		[[Category: Aml]]
	[[Category: Nuclear protein]]		[[Category: Nuclear protein]]

OCA at 04:16, 3 October 2014

OCA — Fri, 03 Oct 2014 04:16:35 GMT

←Older revision		Revision as of 04:16, 3 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2vxd\| PDB=2vxd \| SCENE= }}~~	+	==The structure of the C-terminal domain of Nucleophosmin==
-	===The structure of the C-terminal domain of Nucleophosmin===	+	<StructureSection load='2vxd' size='340' side='right' caption='[[2vxd]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
-	~~{{ABSTRACT_PUBMED_18511415}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[2vxd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VXD FirstGlance]. <br>
-	==Disease==	+	</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=2vxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vxd RCSB], [http://www.ebi.ac.uk/pdbsum/2vxd PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/NPM_HUMAN NPM_HUMAN]] Note=A chromosomal aberration involving NPM1 is found in a form of non-Hodgkin lymphoma. Translocation t(2;5)(p23;q35) with ALK. The resulting chimeric NPM1-ALK protein homodimerize and the kinase becomes constitutively activated. Note=A chromosomal aberration involving NPM1 is found in a form of acute promyelocytic leukemia. Translocation t(5;17)(q32;q11) with RARA. Note=A chromosomal aberration involving NPM1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with MLF1. Note=Defects in NPM1 are associated with acute myelogenous leukemia (AML). Mutations in exon 12 affecting the C-terminus of the protein are associated with an aberrant cytoplasmic location.		[[http://www.uniprot.org/uniprot/NPM_HUMAN NPM_HUMAN]] Note=A chromosomal aberration involving NPM1 is found in a form of non-Hodgkin lymphoma. Translocation t(2;5)(p23;q35) with ALK. The resulting chimeric NPM1-ALK protein homodimerize and the kinase becomes constitutively activated. Note=A chromosomal aberration involving NPM1 is found in a form of acute promyelocytic leukemia. Translocation t(5;17)(q32;q11) with RARA. Note=A chromosomal aberration involving NPM1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with MLF1. Note=Defects in NPM1 are associated with acute myelogenous leukemia (AML). Mutations in exon 12 affecting the C-terminus of the protein are associated with an aberrant cytoplasmic location.
-		+	== Function ==
-	==Function==	+
	[[http://www.uniprot.org/uniprot/NPM_HUMAN NPM_HUMAN]] Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication.<ref>PMID:16107701</ref> <ref>PMID:17015463</ref> <ref>PMID:18809582</ref> <ref>PMID:19188445</ref> <ref>PMID:20352051</ref> <ref>PMID:21084279</ref> <ref>PMID:22002061</ref>		[[http://www.uniprot.org/uniprot/NPM_HUMAN NPM_HUMAN]] Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication.<ref>PMID:16107701</ref> <ref>PMID:17015463</ref> <ref>PMID:18809582</ref> <ref>PMID:19188445</ref> <ref>PMID:20352051</ref> <ref>PMID:21084279</ref> <ref>PMID:22002061</ref>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vx/2vxd_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Mutations affecting nucleophosmin (NPM1) are the most common genetic lesions found in acute myeloid leukaemia (AML). NPM1 is one of the most abundant proteins found in the nucleolus and has links to the MDM2/p53 tumour suppressor pathway. A distinctive feature of NPM1 mutants in AML is their aberrant localization to the cytoplasm of leukaemic cells. This mutant phenotype is the result of the substitution of several C-terminal residues, including one or two conserved tryptophan residues, with a leucine rich nuclear export signal (NES). The exact molecular mechanism underlying the loss of nucleolar retention, and the role of the tryptophans, remains unknown. In this study we have determined the structure of an independently folded globular domain in the C-terminus of NPM1 using NMR spectroscopy and report that the conserved tryptophans are critical for structure. This domain is necessary for the nucleolar targeting of NPM1 and is disrupted by mutations in AML with cytoplasmic NPM1. Furthermore, we identify conserved surface- exposed lysine residues (K263 and K267) that are functionally rather than structurally important for nucleolar localization. This study provides new focus for efforts to understand the pathogenesis of AML with cytoplasmic NPM1 and may be used to aid the design of small molecules that target the C-terminal domain of NPM1 to act as novel anti-proliferative and anti-leukaemia therapeutics.

-	~~==About this Structure==~~	+	Structural consequences of nucleophosmin mutations in acute myeloid leukaemia.,Grummitt CG, Townsley FM, Johnson CM, Warren AJ, Bycroft M J Biol Chem. 2008 May 29;. PMID:18511415<ref>PMID:18511415</ref>
-	~~[[2vxd]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full experimental information is available from [http~~:/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2VXD OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:018511415</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Bycroft, M.]]		[[Category: Bycroft, M.]]

OCA at 11:48, 24 July 2013

OCA — Wed, 24 Jul 2013 11:48:36 GMT

←Older revision		Revision as of 11:48, 24 July 2013
Line 1:		Line 1:
	{{STRUCTURE_2vxd\| PDB=2vxd \| SCENE= }}		{{STRUCTURE_2vxd\| PDB=2vxd \| SCENE= }}
-	===~~THE STRUCTURE OF THE~~ C-~~TERMINAL DOMAIN OF NUCLEOPHOSMIN~~===	+	===The structure of the C-terminal domain of Nucleophosmin===
	{{ABSTRACT_PUBMED_18511415}}		{{ABSTRACT_PUBMED_18511415}}
		+
		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/NPM_HUMAN NPM_HUMAN]] Note=A chromosomal aberration involving NPM1 is found in a form of non-Hodgkin lymphoma. Translocation t(2;5)(p23;q35) with ALK. The resulting chimeric NPM1-ALK protein homodimerize and the kinase becomes constitutively activated. Note=A chromosomal aberration involving NPM1 is found in a form of acute promyelocytic leukemia. Translocation t(5;17)(q32;q11) with RARA. Note=A chromosomal aberration involving NPM1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with MLF1. Note=Defects in NPM1 are associated with acute myelogenous leukemia (AML). Mutations in exon 12 affecting the C-terminus of the protein are associated with an aberrant cytoplasmic location.
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/NPM_HUMAN NPM_HUMAN]] Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication.<ref>PMID:16107701</ref> <ref>PMID:17015463</ref> <ref>PMID:18809582</ref> <ref>PMID:19188445</ref> <ref>PMID:20352051</ref> <ref>PMID:21084279</ref> <ref>PMID:22002061</ref>

	==About this Structure==		==About this Structure==
	[[2vxd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXD OCA].		[[2vxd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXD OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:018511415</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Bycroft, M.]]		[[Category: Bycroft, M.]]

OCA at 03:39, 25 March 2013

OCA — Mon, 25 Mar 2013 03:39:36 GMT

←Older revision		Revision as of 03:39, 25 March 2013
Line 1:		Line 1:
-	[[Image:2vxd.png\|left\|200px]]
-
	{{STRUCTURE_2vxd\| PDB=2vxd \| SCENE= }}		{{STRUCTURE_2vxd\| PDB=2vxd \| SCENE= }}
-
	===THE STRUCTURE OF THE C-TERMINAL DOMAIN OF NUCLEOPHOSMIN===		===THE STRUCTURE OF THE C-TERMINAL DOMAIN OF NUCLEOPHOSMIN===
-
	{{ABSTRACT_PUBMED_18511415}}		{{ABSTRACT_PUBMED_18511415}}

OCA: Protected "2vxd" [edit=sysop:move=sysop]

OCA — Mon, 07 Jan 2013 20:52:53 GMT

Protected "2vxd" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:52, 7 January 2013

OCA at 20:52, 7 January 2013

OCA — Mon, 07 Jan 2013 20:52:50 GMT

←Older revision		Revision as of 20:52, 7 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2vxd.png\|left\|200px]]		[[Image:2vxd.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2vxd", 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_2vxd\| PDB=2vxd \| SCENE= }}		{{STRUCTURE_2vxd\| PDB=2vxd \| SCENE= }}

	===THE STRUCTURE OF THE C-TERMINAL DOMAIN OF NUCLEOPHOSMIN===		===THE STRUCTURE OF THE C-TERMINAL DOMAIN OF NUCLEOPHOSMIN===

		+	{{ABSTRACT_PUBMED_18511415}}

	==About this Structure==		==About this Structure==
-	~~2VXD~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXD OCA].	+	[[2vxd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXD OCA].
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Bycroft, M.]]		[[Category: Bycroft, M.]]
	[[Category: Grummitt, C G.]]		[[Category: Grummitt, C G.]]
-	[[Category: Acetylation]]
-	[[Category: Alternative splicing]]
	[[Category: Aml]]		[[Category: Aml]]
-	[[Category: Chromosomal rearrangement]]
	[[Category: Nuclear protein]]		[[Category: Nuclear protein]]
	[[Category: Nucleolus]]		[[Category: Nucleolus]]
Line 28:		Line 19:
	[[Category: Proto-oncogene]]		[[Category: Proto-oncogene]]
	[[Category: Rna-binding]]		[[Category: Rna-binding]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 07:08:04 2009''