1h2t - Revision history

OCA at 12:15, 13 December 2023

2023-12-13T12:15:41Z

←Older revision		Revision as of 12:15, 13 December 2023
Line 3:		Line 3:
	<StructureSection load='1h2t' size='340' side='right'caption='[[1h2t]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1h2t' size='340' side='right'caption='[[1h2t]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1h2t]] is a 2 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=1H2T OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1H2T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1h2t]] is a 2 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=1H2T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H2T FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=7MG:7N~~-~~METHYL-8-HYDROGUANOSINE-5-MONOPHOSPHATE'>7MG</scene>~~, ~~<scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>~~</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]] 2.1Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[1h6k\|1h6k]]~~, ~~[[1h2u\|1h2u]], [[1h2v\|1h2v]]~~</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7MG:7N-METHYL-8-HYDROGUANOSINE-5-MONOPHOSPHATE'>7MG</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></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=1h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2t OCA], [~~http~~://pdbe.org/1h2t PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1h2t RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1h2t PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1h2t 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=1h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2t OCA], [https://pdbe.org/1h2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h2t RCSB], [https://www.ebi.ac.uk/pdbsum/1h2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h2t ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/NCBP1_HUMAN NCBP1_HUMAN]] Component of the cap-binding complex (CBC), which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5'-end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2 and is required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP1/CBP80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a high affinity cap-binding state with the cap structure.<ref>PMID:8069914</ref> <ref>PMID:7651522</ref> <ref>PMID:11551508</ref> <ref>PMID:15059963</ref> <ref>PMID:15361857</ref> <ref>PMID:16186820</ref> <ref>PMID:17190602</ref> <ref>PMID:16317009</ref> <ref>PMID:17873884</ref> <ref>PMID:18369367</ref> <ref>PMID:19632182</ref> <ref>PMID:19648179</ref> [[http://www.uniprot.org/uniprot/NCBP2_HUMAN NCBP2_HUMAN]] Component of the cap-binding complex (CBC), which binds co-transcriptionally to the 5' cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5' end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2, thereby being required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP2/CBP20 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure.<ref>PMID:11551508</ref> <ref>PMID:15361857</ref> <ref>PMID:17190602</ref> <ref>PMID:17363367</ref> <ref>PMID:17873884</ref> <ref>PMID:18369367</ref> <ref>PMID:19632182</ref>	+	[https://www.uniprot.org/uniprot/NCBP1_HUMAN NCBP1_HUMAN] Component of the cap-binding complex (CBC), which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5'-end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2 and is required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP1/CBP80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a high affinity cap-binding state with the cap structure.<ref>PMID:8069914</ref> <ref>PMID:7651522</ref> <ref>PMID:11551508</ref> <ref>PMID:15059963</ref> <ref>PMID:15361857</ref> <ref>PMID:16186820</ref> <ref>PMID:17190602</ref> <ref>PMID:16317009</ref> <ref>PMID:17873884</ref> <ref>PMID:18369367</ref> <ref>PMID:19632182</ref> <ref>PMID:19648179</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Cusack, S]]	+	[[Category: Cusack S]]
-	[[Category: Mattaj~~, I W~~]]	+	[[Category: Mattaj IW]]
-	[[Category: Mazza, C]]	+	[[Category: Mazza C]]
-	[[Category: Segref, A]]	+	[[Category: Segref A]]
-	~~[[Category: Cap-binding-complex]]~~	+
-	~~[[Category: M7gcap]]~~	+
-	~~[[Category: Mif4g domain]]~~	+
-	~~[[Category: Nuclear protein]]~~	+
-	~~[[Category: Rna export]]~~	+
-	~~[[Category: Rna maturation]]~~	+
-	~~[[Category: Rna-binding]]~~	+
-	~~[[Category: Rnp domain~~]]	+

OCA at 09:17, 6 January 2021

2021-01-06T09:17:31Z

←Older revision		Revision as of 09:17, 6 January 2021
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	<StructureSection load='1h2t' size='340' side='right'caption='[[1h2t]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1h2t' size='340' side='right'caption='[[1h2t]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1h2t]] is a 2 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=1H2T OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1H2T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1h2t]] is a 2 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=1H2T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1H2T FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7MG:7N-METHYL-8-HYDROGUANOSINE-5-MONOPHOSPHATE'>7MG</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7MG:7N-METHYL-8-HYDROGUANOSINE-5-MONOPHOSPHATE'>7MG</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h6k\|1h6k]], [[1h2u\|1h2u]], [[1h2v\|1h2v]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1h6k\|1h6k]], [[1h2u\|1h2u]], [[1h2v\|1h2v]]</div></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=1h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2t OCA], [http://pdbe.org/1h2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h2t RCSB], [http://www.ebi.ac.uk/pdbsum/1h2t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h2t ProSAT]</span></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=1h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2t OCA], [http://pdbe.org/1h2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h2t RCSB], [http://www.ebi.ac.uk/pdbsum/1h2t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h2t ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 07:17, 3 April 2019

2019-04-03T07:17:30Z

←Older revision		Revision as of 07:17, 3 April 2019
Line 1:		Line 1:

	==Structure of the human nuclear cap-binding-complex (CBC) in complex with a cap analogue m7GpppG==		==Structure of the human nuclear cap-binding-complex (CBC) in complex with a cap analogue m7GpppG==
-	<StructureSection load='1h2t' size='340' side='right' caption='[[1h2t]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='1h2t' size='340' side='right'caption='[[1h2t]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1h2t]] is a 2 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=1H2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H2T FirstGlance]. <br>		<table><tr><td colspan='2'>[[1h2t]] is a 2 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=1H2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H2T FirstGlance]. <br>
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h2/1h2t_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h2/1h2t_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 34:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Cusack, S]]		[[Category: Cusack, S]]
	[[Category: Mattaj, I W]]		[[Category: Mattaj, I W]]

OCA at 21:21, 15 November 2017

2017-11-15T21:21:37Z

←Older revision		Revision as of 21:21, 15 November 2017
Line 1:		Line 1:
-	==~~STRUCTURE OF THE HUMAN NUCLEAR CAP~~-~~BINDING~~-~~COMPLEX~~ (CBC) ~~IN COMPLEX WITH A CAP ANALOGUE M7GPPPG~~==	+
		+	==Structure of the human nuclear cap-binding-complex (CBC) in complex with a cap analogue m7GpppG==
	<StructureSection load='1h2t' size='340' side='right' caption='[[1h2t]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1h2t' size='340' side='right' caption='[[1h2t]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7MG:7N-METHYL-8-HYDROGUANOSINE-5-MONOPHOSPHATE'>7MG</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7MG:7N-METHYL-8-HYDROGUANOSINE-5-MONOPHOSPHATE'>7MG</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h6k\|1h6k]], [[1h2u\|1h2u]], [[1h2v\|1h2v]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h6k\|1h6k]], [[1h2u\|1h2u]], [[1h2v\|1h2v]]</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=1h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2t OCA], [http://pdbe.org/1h2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h2t RCSB], [http://www.ebi.ac.uk/pdbsum/1h2t 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=1h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2t OCA], [http://pdbe.org/1h2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h2t RCSB], [http://www.ebi.ac.uk/pdbsum/1h2t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h2t ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 17:12, 7 February 2016

2016-02-07T17:12:55Z

←Older revision		Revision as of 17:12, 7 February 2016
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=1h2t ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 03:32, 10 September 2015

2015-09-10T03:32:04Z

←Older revision		Revision as of 03:32, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1h2t' size='340' side='right' caption='[[1h2t]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1h2t' size='340' side='right' caption='[[1h2t]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1h2t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H2T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1h2t]] is a 2 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=1H2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H2T FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7MG:7N-METHYL-8-HYDROGUANOSINE-5-MONOPHOSPHATE'>7MG</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7MG:7N-METHYL-8-HYDROGUANOSINE-5-MONOPHOSPHATE'>7MG</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h6k\|1h6k]], [[1h2u\|1h2u]], [[1h2v\|1h2v]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h6k\|1h6k]], [[1h2u\|1h2u]], [[1h2v\|1h2v]]</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=1h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h2t RCSB], [http://www.ebi.ac.uk/pdbsum/1h2t 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=1h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2t OCA], [http://pdbe.org/1h2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h2t RCSB], [http://www.ebi.ac.uk/pdbsum/1h2t PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 27:		Line 27:
	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 1h2t" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Cusack, S]]		[[Category: Cusack, S]]
	[[Category: Mattaj, I W]]		[[Category: Mattaj, I W]]

OCA at 16:57, 24 December 2014

2014-12-24T16:57:20Z

←Older revision		Revision as of 16:57, 24 December 2014
Line 7:		Line 7:
	<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=1h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h2t RCSB], [http://www.ebi.ac.uk/pdbsum/1h2t 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=1h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h2t RCSB], [http://www.ebi.ac.uk/pdbsum/1h2t PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/NCBP1_HUMAN NCBP1_HUMAN]] Component of the cap-binding complex (CBC), which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5'-end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2 and is required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP1/CBP80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a high affinity cap-binding state with the cap structure.<ref>PMID:8069914</ref> <ref>PMID:7651522</ref> <ref>PMID:11551508</ref> <ref>PMID:15059963</ref> <ref>PMID:15361857</ref> <ref>PMID:16186820</ref> <ref>PMID:17190602</ref> <ref>PMID:16317009</ref> <ref>PMID:17873884</ref> <ref>PMID:18369367</ref> <ref>PMID:19632182</ref> <ref>PMID:19648179</ref> [[http://www.uniprot.org/uniprot/NCBP2_HUMAN NCBP2_HUMAN]] Component of the cap-binding complex (CBC), which binds co-transcriptionally to the 5' cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5' end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2, thereby being required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP2/CBP20 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure.<ref>PMID:11551508</ref> <ref>PMID:15361857</ref> <ref>PMID:17190602</ref> <ref>PMID:17363367</ref> <ref>PMID:17873884</ref> <ref>PMID:18369367</ref> <ref>PMID:19632182</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 00:33, 23 December 2014

2014-12-23T00:33:19Z

←Older revision		Revision as of 00:33, 23 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1h2t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H2T FirstGlance]. <br>		<table><tr><td colspan='2'>[[1h2t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H2T FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7MG:7N-METHYL-8-HYDROGUANOSINE-5-MONOPHOSPHATE'>7MG</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7MG:7N-METHYL-8-HYDROGUANOSINE-5-MONOPHOSPHATE'>7MG</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h6k\|1h6k]], [[1h2u\|1h2u]], [[1h2v\|1h2v]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h6k\|1h6k]], [[1h2u\|1h2u]], [[1h2v\|1h2v]]</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=1h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h2t RCSB], [http://www.ebi.ac.uk/pdbsum/1h2t 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=1h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h2t RCSB], [http://www.ebi.ac.uk/pdbsum/1h2t PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 30:		Line 30:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Cusack, S.]]	+	[[Category: Cusack, S]]
-	[[Category: Mattaj, I W.]]	+	[[Category: Mattaj, I W]]
-	[[Category: Mazza, C.]]	+	[[Category: Mazza, C]]
-	[[Category: Segref, A.]]	+	[[Category: Segref, A]]
	[[Category: Cap-binding-complex]]		[[Category: Cap-binding-complex]]
	[[Category: M7gcap]]		[[Category: M7gcap]]

OCA at 17:31, 29 September 2014

2014-09-29T17:31:09Z

←Older revision		Revision as of 17:31, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1h2t.~~png~~\|~~left~~\|200px]]	+	==STRUCTURE OF THE HUMAN NUCLEAR CAP-BINDING-COMPLEX (CBC) IN COMPLEX WITH A CAP ANALOGUE M7GPPPG==
		+	<StructureSection load='1h2t' size='340' side='right' caption='[[1h2t]], [[Resolution\|resolution]] 2.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1h2t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H2T FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7MG:7N-METHYL-8-HYDROGUANOSINE-5-MONOPHOSPHATE'>7MG</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h6k\|1h6k]], [[1h2u\|1h2u]], [[1h2v\|1h2v]]</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=1h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h2t RCSB], [http://www.ebi.ac.uk/pdbsum/1h2t PDBsum]</span></td></tr>
		+	<table>
		+	== 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/h2/1h2t_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 ==
		+	The heterodimeric nuclear cap-binding complex (CBC) binds to the 5' cap structure of RNAs in the nucleus and plays a central role in their diverse maturation steps. We describe the crystal structure at 2.1 A resolution of human CBC bound to an m(7)GpppG cap analogue. Comparison with the structure of uncomplexed CBC shows that cap binding induces co-operative folding around the dinucleotide of some 50 residues from the N- and C-terminal extensions to the central RNP domain of the small subunit CBP20. The cap-bound conformation of CBP20 is stabilized by an intricate network of interactions both to the ligand and within the subunit, as well as new interactions of the CBP20 N-terminal tail with the large subunit CBP80. Although the structure is very different from that of other known cap-binding proteins, such as the cytoplasmic cap-binding protein eIF4E, specificity for the methylated guanosine again is achieved by sandwiching the base between two aromatic residues, in this case two conserved tyrosines. Implications for the transfer of capped mRNAs to eIF4E, required for translation initiation, are discussed.

-	~~{{STRUCTURE_1h2t\| PDB=1h2t \| SCENE= }}~~	+	Large-scale induced fit recognition of an m(7)GpppG cap analogue by the human nuclear cap-binding complex.,Mazza C, Segref A, Mattaj IW, Cusack S EMBO J. 2002 Oct 15;21(20):5548-57. PMID:12374755<ref>PMID:12374755</ref>

-	~~===STRUCTURE OF THE HUMAN NUCLEAR CAP-BINDING-COMPLEX (CBC) IN COMPLEX WITH A CAP ANALOGUE M7GPPPG===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_12374755}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1h2t]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1H2T OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:012374755<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Cusack, S.]]		[[Category: Cusack, S.]]

OCA at 09:31, 16 January 2013

2013-01-16T09:31:49Z

←Older revision		Revision as of 09:31, 16 January 2013
Line 1:		Line 1:
	[[Image:1h2t.png\|left\|200px]]		[[Image:1h2t.png\|left\|200px]]

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	{{STRUCTURE_1h2t\| PDB=1h2t \| SCENE= }}		{{STRUCTURE_1h2t\| PDB=1h2t \| SCENE= }}

	===STRUCTURE OF THE HUMAN NUCLEAR CAP-BINDING-COMPLEX (CBC) IN COMPLEX WITH A CAP ANALOGUE M7GPPPG===		===STRUCTURE OF THE HUMAN NUCLEAR CAP-BINDING-COMPLEX (CBC) IN COMPLEX WITH A CAP ANALOGUE M7GPPPG===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_12374755}}, adds the Publication Abstract to the page
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	{{ABSTRACT_PUBMED_12374755}}		{{ABSTRACT_PUBMED_12374755}}

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	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~12374755</ref><ref group="xtra">PMID:12454499~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012374755</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Cusack, S.]]		[[Category: Cusack, S.]]