3rzx - Revision history

OCA at 12:41, 14 March 2024

OCA — Thu, 14 Mar 2024 12:41:28 GMT

←Older revision		Revision as of 12:41, 14 March 2024
Line 3:		Line 3:
	<StructureSection load='3rzx' size='340' side='right'caption='[[3rzx]], [[Resolution\|resolution]] 2.61Å' scene=''>		<StructureSection load='3rzx' size='340' side='right'caption='[[3rzx]], [[Resolution\|resolution]] 2.61Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3rzx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RZX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RZX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3rzx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RZX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RZX FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1q1s\|1q1s]], [[1q1t\|1q1t]], [[1ejy\|1ejy]], [[3l3q\|3l3q]], [[1pjm\|1pjm]], [[1pjn\|1pjn]]</div></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]] 2.61Å</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">Kpna2, Rch1 ([https://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=10090 LK3 transgenic mice])~~</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=3rzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rzx OCA], [https://pdbe.org/3rzx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rzx RCSB], [https://www.ebi.ac.uk/pdbsum/3rzx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rzx 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=3rzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rzx OCA], [https://pdbe.org/3rzx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rzx RCSB], [https://www.ebi.ac.uk/pdbsum/3rzx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rzx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~IMA2_MOUSE IMA2_MOUSE]~~] Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. [[https://www.uniprot.org/uniprot/XRCC6_HUMAN XRCC6_HUMAN]] Single stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. Required for osteocalcin gene expression. Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. 5'-dRP lyase activity allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription.<ref>PMID:2466842</ref> <ref>PMID:8621488</ref> <ref>PMID:7957065</ref> <ref>PMID:9742108</ref> <ref>PMID:12145306</ref> <ref>PMID:20493174</ref> <ref>PMID:20383123</ref>	+	[https://www.uniprot.org/uniprot/IMA1_MOUSE IMA1_MOUSE] Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Ku70 and Ku80 form a heterodimeric complex involved in multiple nuclear processes. This complex plays a key role in DNA repair due to its ability to bind DNA double-strand breaks and facilitate repair by the nonhomologous end-joining pathway. Ku70 and Ku80 have been proposed to contain bipartite and monopartite nuclear localization sequences (NLSs), respectively, that allow them to be translocated to the nucleus independently of each other via the classical importin-alpha (Impalpha)/importin-beta-mediated nuclear import pathway. To determine the structural basis of the recognition of Ku70 and Ku80 proteins by Impalpha, we solved the crystal structures of the complexes of Impalpha with the peptides corresponding to the Ku70 and Ku80 NLSs. Our structural studies confirm the binding of the Ku80 NLS as a classical monopartite NLS but reveal an unexpected binding mode for Ku70 NLS with only one basic cluster bound to the receptor. Both Ku70 and Ku80 therefore contain monopartite NLSs, and sequences outside the basic cluster make favorable interactions with Impalpha, suggesting that this may be a general feature in monopartite NLSs. We show that the Ku70 NLS has a higher affinity for Impalpha than the Ku80 NLS, consistent with more extensive interactions in its N-terminal region. The prospect of nuclear import of Ku70 and Ku80 independently of each other provides a powerful regulatory mechanism for the function of the Ku70/Ku80 heterodimer and independent functions of the two proteins.	+
-		+
-	Structural basis of importin-alpha-mediated nuclear transport for Ku70 and Ku80.,Takeda AA, de Barros AC, Chang CW, Kobe B, Fontes MR J Mol Biol. 2011 Sep 16;412(2):226-34. Epub 2011 Jul 23. PMID:21806995<ref>PMID:21806995</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3rzx" style="background-color:#fffaf0;"></div>~~	+

	==See Also==		==See Also==
	*[[Importin 3D structures\|Importin 3D structures]]		*[[Importin 3D structures\|Importin 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Mus musculus]]
-	[[Category: Fontes~~, M R.M~~]]	+	[[Category: Fontes MRM]]
-	[[Category: Takeda~~, A A.S]]~~	+	[[Category: Takeda AAS]]
-	~~[[Category: Armadillo repeat]]~~	+
-	~~[[Category: Protein transport~~]]	+

OCA at 10:32, 22 June 2022

OCA — Wed, 22 Jun 2022 10:32:06 GMT

←Older revision		Revision as of 10:32, 22 June 2022
Line 1:		Line 1:

	==Mouse importin alpha-Ku70 NLS peptide complex==		==Mouse importin alpha-Ku70 NLS peptide complex==
-	<StructureSection load='3rzx' size='340' side='right' caption='[[3rzx]], [[Resolution\|resolution]] 2.61Å' scene=''>	+	<StructureSection load='3rzx' size='340' side='right'caption='[[3rzx]], [[Resolution\|resolution]] 2.61Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3rzx]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RZX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3RZX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3rzx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RZX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RZX FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1q1s\|1q1s]], [[1q1t\|1q1t]], [[1ejy\|1ejy]], [[3l3q\|3l3q]], [[1pjm\|1pjm]], [[1pjn\|1pjn]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1q1s\|1q1s]], [[1q1t\|1q1t]], [[1ejy\|1ejy]], [[3l3q\|3l3q]], [[1pjm\|1pjm]], [[1pjn\|1pjn]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Kpna2, Rch1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Kpna2, Rch1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3rzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rzx OCA], [~~http~~://pdbe.org/3rzx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3rzx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3rzx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3rzx 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=3rzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rzx OCA], [https://pdbe.org/3rzx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rzx RCSB], [https://www.ebi.ac.uk/pdbsum/3rzx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rzx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/IMA2_MOUSE IMA2_MOUSE]] Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. [[~~http~~://www.uniprot.org/uniprot/XRCC6_HUMAN XRCC6_HUMAN]] Single stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. Required for osteocalcin gene expression. Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. 5'-dRP lyase activity allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription.<ref>PMID:2466842</ref> <ref>PMID:8621488</ref> <ref>PMID:7957065</ref> <ref>PMID:9742108</ref> <ref>PMID:12145306</ref> <ref>PMID:20493174</ref> <ref>PMID:20383123</ref>	+	[[https://www.uniprot.org/uniprot/IMA2_MOUSE IMA2_MOUSE]] Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. [[https://www.uniprot.org/uniprot/XRCC6_HUMAN XRCC6_HUMAN]] Single stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. Required for osteocalcin gene expression. Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. 5'-dRP lyase activity allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription.<ref>PMID:2466842</ref> <ref>PMID:8621488</ref> <ref>PMID:7957065</ref> <ref>PMID:9742108</ref> <ref>PMID:12145306</ref> <ref>PMID:20493174</ref> <ref>PMID:20383123</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 21:

	==See Also==		==See Also==
-	*[[Importin\|Importin]]	+	*[[Importin 3D structures\|Importin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Fontes, M R.M]]		[[Category: Fontes, M R.M]]

OCA at 11:55, 5 August 2016

OCA — Fri, 05 Aug 2016 11:55:28 GMT

←Older revision		Revision as of 11:55, 5 August 2016
Line 1:		Line 1:
		+
	==Mouse importin alpha-Ku70 NLS peptide complex==		==Mouse importin alpha-Ku70 NLS peptide complex==
	<StructureSection load='3rzx' size='340' side='right' caption='[[3rzx]], [[Resolution\|resolution]] 2.61Å' scene=''>		<StructureSection load='3rzx' size='340' side='right' caption='[[3rzx]], [[Resolution\|resolution]] 2.61Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3rzx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RZX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RZX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3rzx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RZX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RZX FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1q1s\|1q1s]], [[1q1t\|1q1t]], [[1ejy\|1ejy]], [[3l3q\|3l3q]], [[1pjm\|1pjm]], [[1pjn\|1pjn]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1q1s\|1q1s]], [[1q1t\|1q1t]], [[1ejy\|1ejy]], [[3l3q\|3l3q]], [[1pjm\|1pjm]], [[1pjn\|1pjn]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Kpna2, Rch1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 ~~Mus musculus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Kpna2, Rch1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3rzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rzx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rzx RCSB], [http://www.ebi.ac.uk/pdbsum/3rzx 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=3rzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rzx OCA], [http://pdbe.org/3rzx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rzx RCSB], [http://www.ebi.ac.uk/pdbsum/3rzx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rzx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		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 3rzx" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 24:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Mus musculus~~]]	+	[[Category: Lk3 transgenic mice]]
	[[Category: Fontes, M R.M]]		[[Category: Fontes, M R.M]]
	[[Category: Takeda, A A.S]]		[[Category: Takeda, A A.S]]
	[[Category: Armadillo repeat]]		[[Category: Armadillo repeat]]
	[[Category: Protein transport]]		[[Category: Protein transport]]

OCA at 02:14, 25 December 2014

OCA — Thu, 25 Dec 2014 02:14:37 GMT

←Older revision		Revision as of 02:14, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3rzx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RZX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RZX FirstGlance]. <br>		<table><tr><td colspan='2'>[[3rzx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RZX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RZX FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1q1s\|1q1s]], [[1q1t\|1q1t]], [[1ejy\|1ejy]], [[3l3q\|3l3q]], [[1pjm\|1pjm]], [[1pjn\|1pjn]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1q1s\|1q1s]], [[1q1t\|1q1t]], [[1ejy\|1ejy]], [[3l3q\|3l3q]], [[1pjm\|1pjm]], [[1pjn\|1pjn]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Kpna2, Rch1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Kpna2, Rch1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=3rzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rzx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rzx RCSB], [http://www.ebi.ac.uk/pdbsum/3rzx 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=3rzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rzx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rzx RCSB], [http://www.ebi.ac.uk/pdbsum/3rzx PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/IMA2_MOUSE IMA2_MOUSE]] Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. [[http://www.uniprot.org/uniprot/XRCC6_HUMAN XRCC6_HUMAN]] Single stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. Required for osteocalcin gene expression. Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. 5'-dRP lyase activity allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription.<ref>PMID:2466842</ref> <ref>PMID:8621488</ref> <ref>PMID:7957065</ref> <ref>PMID:9742108</ref> <ref>PMID:12145306</ref> <ref>PMID:20493174</ref> <ref>PMID:20383123</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 13:		Line 15:
	Structural basis of importin-alpha-mediated nuclear transport for Ku70 and Ku80.,Takeda AA, de Barros AC, Chang CW, Kobe B, Fontes MR J Mol Biol. 2011 Sep 16;412(2):226-34. Epub 2011 Jul 23. PMID:21806995<ref>PMID:21806995</ref>		Structural basis of importin-alpha-mediated nuclear transport for Ku70 and Ku80.,Takeda AA, de Barros AC, Chang CW, Kobe B, Fontes MR J Mol Biol. 2011 Sep 16;412(2):226-34. Epub 2011 Jul 23. PMID:21806995<ref>PMID:21806995</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>
		+
		+	==See Also==
		+	*[[Importin\|Importin]]
	== References ==		== References ==
	<references/>		<references/>
Line 20:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Fontes, M R.M.]]	+	[[Category: Fontes, M R.M]]
-	[[Category: Takeda, A A.S.]]	+	[[Category: Takeda, A A.S]]
	[[Category: Armadillo repeat]]		[[Category: Armadillo repeat]]
	[[Category: Protein transport]]		[[Category: Protein transport]]

OCA at 04:44, 5 June 2014

OCA — Thu, 05 Jun 2014 04:44:16 GMT

←Older revision		Revision as of 04:44, 5 June 2014
Line 1:		Line 1:
-	[[~~Image:~~3rzx.~~png~~\|~~left~~\|~~200px~~]]	+	==Mouse importin alpha-Ku70 NLS peptide complex==
		+	<StructureSection load='3rzx' size='340' side='right' caption='[[3rzx]], [[Resolution\|resolution]] 2.61Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3rzx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RZX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RZX FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1q1s\|1q1s]], [[1q1t\|1q1t]], [[1ejy\|1ejy]], [[3l3q\|3l3q]], [[1pjm\|1pjm]], [[1pjn\|1pjn]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Kpna2, Rch1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=3rzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rzx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rzx RCSB], [http://www.ebi.ac.uk/pdbsum/3rzx PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Ku70 and Ku80 form a heterodimeric complex involved in multiple nuclear processes. This complex plays a key role in DNA repair due to its ability to bind DNA double-strand breaks and facilitate repair by the nonhomologous end-joining pathway. Ku70 and Ku80 have been proposed to contain bipartite and monopartite nuclear localization sequences (NLSs), respectively, that allow them to be translocated to the nucleus independently of each other via the classical importin-alpha (Impalpha)/importin-beta-mediated nuclear import pathway. To determine the structural basis of the recognition of Ku70 and Ku80 proteins by Impalpha, we solved the crystal structures of the complexes of Impalpha with the peptides corresponding to the Ku70 and Ku80 NLSs. Our structural studies confirm the binding of the Ku80 NLS as a classical monopartite NLS but reveal an unexpected binding mode for Ku70 NLS with only one basic cluster bound to the receptor. Both Ku70 and Ku80 therefore contain monopartite NLSs, and sequences outside the basic cluster make favorable interactions with Impalpha, suggesting that this may be a general feature in monopartite NLSs. We show that the Ku70 NLS has a higher affinity for Impalpha than the Ku80 NLS, consistent with more extensive interactions in its N-terminal region. The prospect of nuclear import of Ku70 and Ku80 independently of each other provides a powerful regulatory mechanism for the function of the Ku70/Ku80 heterodimer and independent functions of the two proteins.

-	<!--	+	Structural basis of importin-alpha-mediated nuclear transport for Ku70 and Ku80.,Takeda AA, de Barros AC, Chang CW, Kobe B, Fontes MR J Mol Biol. 2011 Sep 16;412(2):226-34. Epub 2011 Jul 23. PMID:21806995<ref>PMID:21806995</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_3rzx"~~, ~~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_3rzx\| PDB=3rzx \| SCENE= }}~~	+

-	~~===Mouse importin alpha-Ku70 NLS peptide complex===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~<!--~~	+	<references/>
-	~~The line below this paragraph~~, ~~{{ABSTRACT_PUBMED_21806995}}, adds~~ the ~~Publication Abstract to the page~~	+	__TOC__
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 21806995 is the PubMed ID number~~.	+	</StructureSection>
-	-->	+
-	~~{{ABSTRACT_PUBMED_21806995}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3rzx]] is a 2 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RZX OCA].~~	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:021806995<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Fontes, M R.M.]]		[[Category: Fontes, M R.M.]]

OCA at 05:11, 23 May 2012

OCA — Wed, 23 May 2012 05:11:06 GMT

←Older revision		Revision as of 05:11, 23 May 2012
Line 1:		Line 1:
-	[[Image:3rzx.~~jpg~~\|left\|200px]]	+	[[Image:3rzx.png\|left\|200px]]

	<!--		<!--
Line 11:		Line 11:
	===Mouse importin alpha-Ku70 NLS peptide complex===		===Mouse importin alpha-Ku70 NLS peptide complex===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21806995}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21806995 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21806995}}

	==About this Structure==		==About this Structure==
	[[3rzx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RZX OCA].		[[3rzx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RZX OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021806995</ref><references group="xtra"/>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Fontes, M R.M.]]		[[Category: Fontes, M R.M.]]

OCA at 09:01, 3 August 2011

OCA — Wed, 03 Aug 2011 09:01:13 GMT

←Older revision		Revision as of 09:01, 3 August 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3rzx.jpg\|left\|200px]]

-	The ~~entry 3rzx~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3rzx", 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_3rzx\| PDB=3rzx \| SCENE= }}

-	~~Authors: Takeda, A.A.S., Fontes, M.R.M.~~	+	===Mouse importin alpha-Ku70 NLS peptide complex===

-	~~Description~~: ~~Mouse importin alpha~~-~~Ku70 NLS peptide complex~~	+
		+	==About this Structure==
		+	[[3rzx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RZX OCA].
		+	[[Category: Mus musculus]]
		+	[[Category: Fontes, M R.M.]]
		+	[[Category: Takeda, A A.S.]]
		+	[[Category: Armadillo repeat]]
		+	[[Category: Protein transport]]

OCA at 06:08, 20 July 2011

OCA — Wed, 20 Jul 2011 06:08:54 GMT

←Older revision		Revision as of 06:08, 20 July 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3rzx is ON HOLD until ~~May 12 2013~~	+	The entry 3rzx is ON HOLD until Paper Publication

	Authors: Takeda, A.A.S., Fontes, M.R.M.		Authors: Takeda, A.A.S., Fontes, M.R.M.

	Description: Mouse importin alpha-Ku70 NLS peptide complex		Description: Mouse importin alpha-Ku70 NLS peptide complex

OCA at 05:53, 15 June 2011

OCA — Wed, 15 Jun 2011 05:53:22 GMT

←Older revision		Revision as of 05:53, 15 June 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3rzx is ON HOLD	+	The entry 3rzx is ON HOLD until May 12 2013

	Authors: Takeda, A.A.S., Fontes, M.R.M.		Authors: Takeda, A.A.S., Fontes, M.R.M.

	Description: Mouse importin alpha-Ku70 NLS peptide complex		Description: Mouse importin alpha-Ku70 NLS peptide complex

OCA: Protected "3rzx" [edit=sysop:move=sysop]

OCA — Wed, 18 May 2011 05:20:51 GMT

Protected "3rzx" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:20, 18 May 2011