3loz - Revision history

OCA at 08:46, 7 February 2024

OCA — Wed, 07 Feb 2024 08:46:49 GMT

←Older revision		Revision as of 08:46, 7 February 2024
Line 3:		Line 3:
	<StructureSection load='3loz' size='340' side='right'caption='[[3loz]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='3loz' size='340' side='right'caption='[[3loz]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3loz]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LOZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LOZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3loz]] is a 4 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=3LOZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LOZ 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;'>~~[[~~3low~~\|~~3low~~]]~~</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]] 1.8Å</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=3loz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3loz OCA], [https://pdbe.org/3loz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3loz RCSB], [https://www.ebi.ac.uk/pdbsum/3loz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3loz 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=3loz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3loz OCA], [https://pdbe.org/3loz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3loz RCSB], [https://www.ebi.ac.uk/pdbsum/3loz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3loz ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:[https://omim.org/entry/241600 241600]]. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation.<ref>PMID:16549777</ref> Note=Beta-2-microglobulin may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. Persistently high beta(2)-microglobulin serum levels lead to amyloidosis in patients on long-term hemodialysis.<ref>PMID:3532124</ref> <ref>PMID:1336137</ref> <ref>PMID:7554280</ref> <ref>PMID:4586824</ref> <ref>PMID:8084451</ref> <ref>PMID:12119416</ref> <ref>PMID:12796775</ref> <ref>PMID:16901902</ref> <ref>PMID:16491088</ref> <ref>PMID:17646174</ref> <ref>PMID:18835253</ref> <ref>PMID:18395224</ref> <ref>PMID:19284997</ref>	+	[https://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:[https://omim.org/entry/241600 241600]. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation.<ref>PMID:16549777</ref> Note=Beta-2-microglobulin may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. Persistently high beta(2)-microglobulin serum levels lead to amyloidosis in patients on long-term hemodialysis.<ref>PMID:3532124</ref> <ref>PMID:1336137</ref> <ref>PMID:7554280</ref> <ref>PMID:4586824</ref> <ref>PMID:8084451</ref> <ref>PMID:12119416</ref> <ref>PMID:12796775</ref> <ref>PMID:16901902</ref> <ref>PMID:16491088</ref> <ref>PMID:17646174</ref> <ref>PMID:18835253</ref> <ref>PMID:18395224</ref> <ref>PMID:19284997</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.	+	[https://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	beta-microglobulin (betam) is the light chain of the type I major histocompatibility complex. It deposits as amyloid fibrils within joints during long-term hemodialysis treatment. Despite the devastating effects of dialysis-related amyloidosis, full understanding of how fibrils form from soluble betam remains elusive. Here we show that betam can oligomerize and fibrillize via three-dimensional domain swapping. Isolating a covalently bound, domain-swapped dimer from betam oligomers on the pathway to fibrils, we were able to determine its crystal structure. The hinge loop that connects the swapped domain to the core domain includes the fibrillizing segment LSFSKD, whose atomic structure we also determined. The LSFSKD structure reveals a class 5 steric zipper, akin to other amyloid spines. The structures of the dimer and the zipper spine fit well into an atomic model for this fibrillar form of betam, which assembles slowly under physiological conditions.	+
-		+
-	beta-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages.,Liu C, Sawaya MR, Eisenberg D Nat Struct Mol Biol. 2011 Jan;18(1):49-55. Epub 2010 Dec 5. PMID:21131979<ref>PMID:21131979</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3loz" style="background-color:#fffaf0;"></div>~~	+

	==See Also==		==See Also==
Line 27:		Line 18:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Eisenberg, D]]	+	[[Category: Eisenberg D]]
-	[[Category: Liu, C]]	+	[[Category: Liu C]]
-	[[Category: Sawaya, M]]	+	[[Category: Sawaya M]]
-	~~[[Category: Beta 2 microglobulin]]~~	+
-	~~[[Category: Beta spine]]~~	+
-	~~[[Category: Protein fibril]]~~	+
-	~~[[Category: Steric zipper~~]]	+

OCA at 13:41, 4 May 2022

OCA — Wed, 04 May 2022 13:41:44 GMT

←Older revision		Revision as of 13:41, 4 May 2022
Line 3:		Line 3:
	<StructureSection load='3loz' size='340' side='right'caption='[[3loz]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='3loz' size='340' side='right'caption='[[3loz]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3loz]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LOZ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3LOZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3loz]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LOZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LOZ FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3low\|3low]]</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;'>[[3low\|3low]]</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=3loz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3loz OCA], [~~http~~://pdbe.org/3loz PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3loz RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3loz PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3loz 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=3loz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3loz OCA], [https://pdbe.org/3loz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3loz RCSB], [https://www.ebi.ac.uk/pdbsum/3loz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3loz ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:[~~http~~://omim.org/entry/241600 241600]]. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation.<ref>PMID:16549777</ref> Note=Beta-2-microglobulin may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. Persistently high beta(2)-microglobulin serum levels lead to amyloidosis in patients on long-term hemodialysis.<ref>PMID:3532124</ref> <ref>PMID:1336137</ref> <ref>PMID:7554280</ref> <ref>PMID:4586824</ref> <ref>PMID:8084451</ref> <ref>PMID:12119416</ref> <ref>PMID:12796775</ref> <ref>PMID:16901902</ref> <ref>PMID:16491088</ref> <ref>PMID:17646174</ref> <ref>PMID:18835253</ref> <ref>PMID:18395224</ref> <ref>PMID:19284997</ref>	+	[[https://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:[https://omim.org/entry/241600 241600]]. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation.<ref>PMID:16549777</ref> Note=Beta-2-microglobulin may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. Persistently high beta(2)-microglobulin serum levels lead to amyloidosis in patients on long-term hemodialysis.<ref>PMID:3532124</ref> <ref>PMID:1336137</ref> <ref>PMID:7554280</ref> <ref>PMID:4586824</ref> <ref>PMID:8084451</ref> <ref>PMID:12119416</ref> <ref>PMID:12796775</ref> <ref>PMID:16901902</ref> <ref>PMID:16491088</ref> <ref>PMID:17646174</ref> <ref>PMID:18835253</ref> <ref>PMID:18395224</ref> <ref>PMID:19284997</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.	+	[[https://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 07:17, 7 August 2019

OCA — Wed, 07 Aug 2019 07:17:13 GMT

←Older revision		Revision as of 07:17, 7 August 2019
Line 1:		Line 1:

	==Crystal structure of Beta 2 Microglobulin amyloidogenic segment LSFSKD==		==Crystal structure of Beta 2 Microglobulin amyloidogenic segment LSFSKD==
-	<StructureSection load='3loz' size='340' side='right' caption='[[3loz]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='3loz' size='340' side='right'caption='[[3loz]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3loz]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LOZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LOZ FirstGlance]. <br>		<table><tr><td colspan='2'>[[3loz]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LOZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LOZ FirstGlance]. <br>
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 3loz" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3loz" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Beta-2 microglobulin 3D structures\|Beta-2 microglobulin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Eisenberg, D]]		[[Category: Eisenberg, D]]
	[[Category: Liu, C]]		[[Category: Liu, C]]

OCA at 09:00, 1 November 2017

OCA — Wed, 01 Nov 2017 09:00:19 GMT

←Older revision		Revision as of 09:00, 1 November 2017
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 3loz" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3loz" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Beta-2 microglobulin\|Beta-2 microglobulin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 16:41, 4 August 2016

OCA — Thu, 04 Aug 2016 16:41:28 GMT

←Older revision		Revision as of 16:41, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of Beta 2 Microglobulin amyloidogenic segment LSFSKD==		==Crystal structure of Beta 2 Microglobulin amyloidogenic segment LSFSKD==
	<StructureSection load='3loz' size='340' side='right' caption='[[3loz]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='3loz' size='340' side='right' caption='[[3loz]], [[Resolution\|resolution]] 1.80Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[3loz]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LOZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LOZ FirstGlance]. <br>		<table><tr><td colspan='2'>[[3loz]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LOZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LOZ FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3low\|3low]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3low\|3low]]</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=3loz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3loz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3loz RCSB], [http://www.ebi.ac.uk/pdbsum/3loz 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=3loz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3loz OCA], [http://pdbe.org/3loz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3loz RCSB], [http://www.ebi.ac.uk/pdbsum/3loz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3loz ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 18:		Line 19:
	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 3loz" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 17:58, 18 December 2014

OCA — Thu, 18 Dec 2014 17:58:11 GMT

←Older revision		Revision as of 17:58, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3loz\| PDB~~=3loz \| ~~SCENE~~= }}	+	==Crystal structure of Beta 2 Microglobulin amyloidogenic segment LSFSKD==
-	===~~Crystal~~ structure of Beta 2 ~~Microglobulin amyloidogenic segment LSFSKD~~===	+	<StructureSection load='3loz' size='340' side='right' caption='[[3loz]], [[Resolution\|resolution]] 1.80Å' scene=''>
-	~~{{ABSTRACT_PUBMED_21131979}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3loz]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LOZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LOZ FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3low\|3low]]</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=3loz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3loz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3loz RCSB], [http://www.ebi.ac.uk/pdbsum/3loz PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:[http://omim.org/entry/241600 241600]]. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation.<ref>PMID:16549777</ref> Note=Beta-2-microglobulin may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. Persistently high beta(2)-microglobulin serum levels lead to amyloidosis in patients on long-term hemodialysis.<ref>PMID:3532124</ref> <ref>PMID:1336137</ref> <ref>PMID:7554280</ref> <ref>PMID:4586824</ref> <ref>PMID:8084451</ref> <ref>PMID:12119416</ref> <ref>PMID:12796775</ref> <ref>PMID:16901902</ref> <ref>PMID:16491088</ref> <ref>PMID:17646174</ref> <ref>PMID:18835253</ref> <ref>PMID:18395224</ref> <ref>PMID:19284997</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	beta-microglobulin (betam) is the light chain of the type I major histocompatibility complex. It deposits as amyloid fibrils within joints during long-term hemodialysis treatment. Despite the devastating effects of dialysis-related amyloidosis, full understanding of how fibrils form from soluble betam remains elusive. Here we show that betam can oligomerize and fibrillize via three-dimensional domain swapping. Isolating a covalently bound, domain-swapped dimer from betam oligomers on the pathway to fibrils, we were able to determine its crystal structure. The hinge loop that connects the swapped domain to the core domain includes the fibrillizing segment LSFSKD, whose atomic structure we also determined. The LSFSKD structure reveals a class 5 steric zipper, akin to other amyloid spines. The structures of the dimer and the zipper spine fit well into an atomic model for this fibrillar form of betam, which assembles slowly under physiological conditions.

-	~~==Disease==~~	+	beta-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages.,Liu C, Sawaya MR, Eisenberg D Nat Struct Mol Biol. 2011 Jan;18(1):49-55. Epub 2010 Dec 5. PMID:21131979<ref>PMID:21131979</ref>
-	[[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:[http://omim.org/entry/241600 241600]]. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation.<ref>PMID:16549777</ref> Note=Beta-2-~~microglobulin may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into~~ amyloid fibrils ~~is concentration dependent~~. ~~Persistently high beta~~(2)-~~microglobulin serum levels lead to amyloidosis in patients on long-term hemodialysis~~.~~<ref>~~PMID:3532124</ref><ref>PMID:1336137</ref><ref>PMID:7554280</ref><ref>PMID:4586824</ref><ref>PMID:8084451</ref><ref>PMID:12119416</ref><ref>PMID:12796775</ref><ref>PMID:16901902</ref><ref>PMID:16491088</ref><ref>PMID:17646174</ref><ref>PMID:18835253</ref><ref>PMID:18395224</ref><ref>PMID:~~19284997~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Component~~ of the ~~class I major histocompatibility complex (MHC)~~. ~~Involved in the presentation~~ of ~~peptide antigens to the immune system~~.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[3loz]] is a 4 chain structure. Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3LOZ OCA].~~	+

	==See Also==		==See Also==
	*[[Beta-2 microglobulin\|Beta-2 microglobulin]]		*[[Beta-2 microglobulin\|Beta-2 microglobulin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:021131979</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
-	[[Category: Eisenberg, D.]]	+	</StructureSection>
-	[[Category: Liu, C.]]	+	[[Category: Eisenberg, D]]
-	[[Category: Sawaya, M.]]	+	[[Category: Liu, C]]
		+	[[Category: Sawaya, M]]
	[[Category: Beta 2 microglobulin]]		[[Category: Beta 2 microglobulin]]
	[[Category: Beta spine]]		[[Category: Beta spine]]
	[[Category: Protein fibril]]		[[Category: Protein fibril]]
	[[Category: Steric zipper]]		[[Category: Steric zipper]]

OCA at 22:32, 24 March 2013

OCA — Sun, 24 Mar 2013 22:32:31 GMT

←Older revision		Revision as of 22:32, 24 March 2013
Line 1:		Line 1:
-	[[Image:3loz.png\|left\|200px]]
-
	{{STRUCTURE_3loz\| PDB=3loz \| SCENE= }}		{{STRUCTURE_3loz\| PDB=3loz \| SCENE= }}
-
	===Crystal structure of Beta 2 Microglobulin amyloidogenic segment LSFSKD===		===Crystal structure of Beta 2 Microglobulin amyloidogenic segment LSFSKD===
		+	{{ABSTRACT_PUBMED_21131979}}

-	~~{{ABSTRACT_PUBMED_21131979}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:[http://omim.org/entry/241600 241600]]. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation.<ref>PMID:16549777</ref> Note=Beta-2-microglobulin may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. Persistently high beta(2)-microglobulin serum levels lead to amyloidosis in patients on long-term hemodialysis.<ref>PMID:3532124</ref><ref>PMID:1336137</ref><ref>PMID:7554280</ref><ref>PMID:4586824</ref><ref>PMID:8084451</ref><ref>PMID:12119416</ref><ref>PMID:12796775</ref><ref>PMID:16901902</ref><ref>PMID:16491088</ref><ref>PMID:17646174</ref><ref>PMID:18835253</ref><ref>PMID:18395224</ref><ref>PMID:19284997</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:021131979</ref><references group="xtra"/>	+	<ref group="xtra">PMID:021131979</ref><references group="xtra"/><references/>
	[[Category: Eisenberg, D.]]		[[Category: Eisenberg, D.]]
	[[Category: Liu, C.]]		[[Category: Liu, C.]]

OCA at 07:24, 20 October 2012

OCA — Sat, 20 Oct 2012 07:24:22 GMT

←Older revision		Revision as of 07:24, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3loz]] is a 4 chain structure ~~of [[Beta-2 microglobulin]]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LOZ OCA].	+	[[3loz]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LOZ OCA].

	==See Also==		==See Also==

OCA at 06:26, 19 September 2012

OCA — Wed, 19 Sep 2012 06:26:36 GMT

←Older revision		Revision as of 06:26, 19 September 2012
Line 5:		Line 5:
	===Crystal structure of Beta 2 Microglobulin amyloidogenic segment LSFSKD===		===Crystal structure of Beta 2 Microglobulin amyloidogenic segment LSFSKD===

-	{{~~ABSTRACT_PUBMED_021131979~~}}	+	{{ABSTRACT_PUBMED_21131979}}

	==About this Structure==		==About this Structure==

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

OCA — Wed, 25 Jul 2012 16:12:27 GMT

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

←Older revision

Revision as of 16:12, 25 July 2012