8fua - Revision history

OCA at 07:46, 23 August 2023

OCA — Wed, 23 Aug 2023 07:46:59 GMT

←Older revision		Revision as of 07:46, 23 August 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[8fua]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Hendra_virus_horse/Australia/Hendra/1994 Hendra virus horse/Australia/Hendra/1994] 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=8FUA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FUA FirstGlance]. <br>		<table><tr><td colspan='2'>[[8fua]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Hendra_virus_horse/Australia/Hendra/1994 Hendra virus horse/Australia/Hendra/1994] 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=8FUA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FUA FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8fua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fua OCA], [https://pdbe.org/8fua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fua RCSB], [https://www.ebi.ac.uk/pdbsum/8fua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fua ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.9Å</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=8fua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fua OCA], [https://pdbe.org/8fua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fua RCSB], [https://www.ebi.ac.uk/pdbsum/8fua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fua ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[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.		[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.
		+
		+	==See Also==
		+	*[[Importin 3D structures\|Importin 3D structures]]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 06:49, 8 February 2023

OCA — Wed, 08 Feb 2023 06:49:03 GMT

←Older revision		Revision as of 06:49, 8 February 2023
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 8fua ~~is ON HOLD~~	+	==Crystal structure of mouse Importin alpha in complex with Hendra virus matrix protein NLS1==
-		+	<StructureSection load='8fua' size='340' side='right'caption='[[8fua]], [[Resolution\|resolution]] 1.90Å' scene=''>
-	~~Authors~~: ~~Donnelly~~, C.M., ~~Basler~~, C.F., ~~Scott, C~~., ~~Forwood, J~~.K.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[8fua]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Hendra_virus_horse/Australia/Hendra/1994 Hendra virus horse/Australia/Hendra/1994] 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=8FUA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FUA FirstGlance]. <br>
-	~~Description~~: ~~Crystal structure of mouse Importin alpha~~ in complex ~~with~~ Hendra virus ~~matrix protein NLS1~~	+	</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=8fua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fua OCA], [https://pdbe.org/8fua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fua RCSB], [https://www.ebi.ac.uk/pdbsum/8fua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fua ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: ~~Forwood, J.K~~]]	+	== Function ==
-	[[Category: ~~Scott, C~~]]	+	[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.
-	[[Category: ~~Basler, C.F~~]]	+	__TOC__
-	[[Category: ~~Donnelly,~~ C.M]]	+	</StructureSection>
		+	[[Category: Hendra virus horse/Australia/Hendra/1994]]
		+	[[Category: Large Structures]]
		+	[[Category: Mus musculus]]
		+	[[Category: Basler CF]]
		+	[[Category: Donnelly CM]]
		+	[[Category: Forwood JK]]
		+	[[Category: Scott C]]

OCA: Protected "8fua" [edit=sysop:move=sysop]

OCA — Wed, 25 Jan 2023 04:59:50 GMT

Protected "8fua" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:59, 25 January 2023

OCA: New page: '''Unreleased structure''' The entry 8fua is ON HOLD Authors: Donnelly, C.M., Basler, C.F., Scott, C., Forwood, J.K. Description: Crystal structure of mouse Importin alpha in complex w...

OCA — Wed, 25 Jan 2023 04:59:48 GMT

New page: '''Unreleased structure''' The entry 8fua is ON HOLD Authors: Donnelly, C.M., Basler, C.F., Scott, C., Forwood, J.K. Description: Crystal structure of mouse Importin alpha in complex w...

New page

'''Unreleased structure'''

The entry 8fua is ON HOLD

Authors: Donnelly, C.M., Basler, C.F., Scott, C., Forwood, J.K.

Description: Crystal structure of mouse Importin alpha in complex with Hendra virus matrix protein NLS1
[[Category: Unreleased Structures]]
[[Category: Forwood, J.K]]
[[Category: Scott, C]]
[[Category: Basler, C.F]]
[[Category: Donnelly, C.M]]