6dfm - Revision history

OCA at 14:33, 13 March 2024

OCA — Wed, 13 Mar 2024 14:33:57 GMT

←Older revision		Revision as of 14:33, 13 March 2024
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	<StructureSection load='6dfm' size='340' side='right'caption='[[6dfm]], [[Resolution\|resolution]] 2.14Å' scene=''>		<StructureSection load='6dfm' size='340' side='right'caption='[[6dfm]], [[Resolution\|resolution]] 2.14Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6dfm]] 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=6DFM OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6DFM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6dfm]] 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=6DFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DFM FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=3BH:(2R~~,~~3R,4S,5R)-~~2~~-(6,8-DIAMINOPURIN-9-YL)-5-(HYDROXYMETHYL)OXOLANE-3,4-DIOL'>3BH</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]] 2.14Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>HSPA5, GRP78 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id~~=9606 HUMAN])</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3BH:(2R,3R,4S,5R)-2-(6,8-DIAMINOPURIN-9-YL)-5-(HYDROXYMETHYL)OXOLANE-3,4-DIOL'>3BH</scene></td></tr>
-	~~<tr id='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[http~~:~~//en.wikipedia.org/wiki/Non~~-~~chaperonin_molecular_chaperone_ATPase Non~~-~~chaperonin molecular chaperone ATPase]~~, ~~with EC number [http://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=~~3~~.6.~~4~~.10 3.6.4.10]~~ </~~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=6dfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dfm OCA], [https://pdbe.org/6dfm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dfm RCSB], [https://www.ebi.ac.uk/pdbsum/6dfm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dfm ProSAT]</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=6dfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dfm OCA], [~~http~~://pdbe.org/6dfm PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6dfm RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6dfm PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6dfm ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/BIP_HUMAN BIP_HUMAN]] Autoantigen in rheumatoid arthritis.<ref>PMID:11160188</ref>	+	[https://www.uniprot.org/uniprot/BIP_HUMAN BIP_HUMAN] Autoantigen in rheumatoid arthritis.<ref>PMID:11160188</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/BIP_HUMAN BIP_HUMAN]] Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (PubMed:2294010, PubMed:23769672, PubMed:23990668, PubMed:28332555). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (PubMed:1550958, PubMed:19538957). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1 (By similarity). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 (By similarity). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating.[UniProtKB:G3I8R9][UniProtKB:P20029]<ref>PMID:1550958</ref> <ref>PMID:19538957</ref> <ref>PMID:2294010</ref> <ref>PMID:23769672</ref> <ref>PMID:23990668</ref> <ref>PMID:28332555</ref> <ref>PMID:29719251</ref>	+	[https://www.uniprot.org/uniprot/BIP_HUMAN BIP_HUMAN] Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (PubMed:2294010, PubMed:23769672, PubMed:23990668, PubMed:28332555). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (PubMed:1550958, PubMed:19538957). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1 (By similarity). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 (By similarity). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating.[UniProtKB:G3I8R9][UniProtKB:P20029]<ref>PMID:1550958</ref> <ref>PMID:19538957</ref> <ref>PMID:2294010</ref> <ref>PMID:23769672</ref> <ref>PMID:23990668</ref> <ref>PMID:28332555</ref> <ref>PMID:29719251</ref>
		+
		+	==See Also==
		+	*[[Heat Shock Protein structures\|Heat Shock Protein structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Non-chaperonin molecular chaperone ATPase]]~~	+	[[Category: Antoshchenko T]]
-	[[Category: Antoshchenko, T]]	+	[[Category: Chen Y]]
-	[[Category: Chen, Y]]	+	[[Category: Cooney OM]]
-	[[Category: Cooney~~, O M~~]]	+	[[Category: Ferrie RP]]
-	[[Category: Ferrie~~, R P~~]]	+	[[Category: Huang Y]]
-	[[Category: Huang, Y]]	+	[[Category: Park HW]]
-	[[Category: Park~~, H W]]~~	+
-	~~[[Category: Chaperone]]~~	+
-	~~[[Category: Endoplasmic reticulum]]~~	+
-	~~[[Category: Nucleoside analog]]~~	+
-	~~[[Category: Unfolded protein response~~]]	+

OCA at 07:23, 21 May 2019

OCA — Tue, 21 May 2019 07:23:10 GMT

←Older revision		Revision as of 07:23, 21 May 2019
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6dfm is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Crystal structure of human GRP78 in complex with 8-aminoadenosine==
-		+	<StructureSection load='6dfm' size='340' side='right'caption='[[6dfm]], [[Resolution\|resolution]] 2.14Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6dfm]] 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=6DFM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DFM FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3BH:(2R,3R,4S,5R)-2-(6,8-DIAMINOPURIN-9-YL)-5-(HYDROXYMETHYL)OXOLANE-3,4-DIOL'>3BH</scene></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HSPA5, GRP78 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-chaperonin_molecular_chaperone_ATPase Non-chaperonin molecular chaperone ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.10 3.6.4.10] </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=6dfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dfm OCA], [http://pdbe.org/6dfm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dfm RCSB], [http://www.ebi.ac.uk/pdbsum/6dfm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dfm ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/BIP_HUMAN BIP_HUMAN]] Autoantigen in rheumatoid arthritis.<ref>PMID:11160188</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/BIP_HUMAN BIP_HUMAN]] Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (PubMed:2294010, PubMed:23769672, PubMed:23990668, PubMed:28332555). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (PubMed:1550958, PubMed:19538957). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1 (By similarity). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 (By similarity). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating.[UniProtKB:G3I8R9][UniProtKB:P20029]<ref>PMID:1550958</ref> <ref>PMID:19538957</ref> <ref>PMID:2294010</ref> <ref>PMID:23769672</ref> <ref>PMID:23990668</ref> <ref>PMID:28332555</ref> <ref>PMID:29719251</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
		+	[[Category: Non-chaperonin molecular chaperone ATPase]]
		+	[[Category: Antoshchenko, T]]
		+	[[Category: Chen, Y]]
		+	[[Category: Cooney, O M]]
		+	[[Category: Ferrie, R P]]
		+	[[Category: Huang, Y]]
		+	[[Category: Park, H W]]
		+	[[Category: Chaperone]]
		+	[[Category: Endoplasmic reticulum]]
		+	[[Category: Nucleoside analog]]
		+	[[Category: Unfolded protein response]]

OCA at 05:47, 25 July 2018

OCA — Wed, 25 Jul 2018 05:47:20 GMT

←Older revision		Revision as of 05:47, 25 July 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6dfm is ON HOLD	+	The entry 6dfm is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "6dfm" [edit=sysop:move=sysop]

OCA — Wed, 23 May 2018 06:03:21 GMT

Protected "6dfm" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:03, 23 May 2018

OCA: New page: '''Unreleased structure''' The entry 6dfm is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 23 May 2018 06:03:20 GMT

New page: '''Unreleased structure''' The entry 6dfm is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6dfm is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]