4rms - Revision history

OCA at 17:52, 20 September 2023

OCA — Wed, 20 Sep 2023 17:52:21 GMT

←Older revision		Revision as of 17:52, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4rms]] is a 1 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=4RMS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RMS FirstGlance]. <br>		<table><tr><td colspan='2'>[[4rms]] is a 1 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=4RMS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RMS FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 1.7Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=4rms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rms OCA], [https://pdbe.org/4rms PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rms RCSB], [https://www.ebi.ac.uk/pdbsum/4rms PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rms 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=4rms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rms OCA], [https://pdbe.org/4rms PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rms RCSB], [https://www.ebi.ac.uk/pdbsum/4rms PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rms ProSAT]</span></td></tr>
	</table>		</table>

OCA at 07:04, 2 March 2023

OCA — Thu, 02 Mar 2023 07:04:58 GMT

←Older revision		Revision as of 07:04, 2 March 2023
Line 3:		Line 3:
	<StructureSection load='4rms' size='340' side='right'caption='[[4rms]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='4rms' size='340' side='right'caption='[[4rms]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4rms]] is a 1 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=4RMS OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4RMS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4rms]] is a 1 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=4RMS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RMS FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2yxf\|2yxf]], [[4fxl\|4fxl]], [[4rmq\|4rmq]], [[4rmr\|4rmr]], [[4rmt\|4rmt]], [[4rmu\|4rmu]], [[4rmv\|4rmv]], [[4rmw\|4rmw]]</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=4rms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rms OCA], [https://pdbe.org/4rms PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rms RCSB], [https://www.ebi.ac.uk/pdbsum/4rms PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rms ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B2M, CDABP0092, HDCMA22P, NM_004048 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4rms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rms OCA], [~~http~~://pdbe.org/4rms PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4rms RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4rms PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4rms 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 ==
Line 29:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bolognesi, M]]	+	[[Category: Bolognesi M]]
-	[[Category: Ricagno, S]]	+	[[Category: Ricagno S]]
-	[[Category: Rosa, M ~~de]]~~	+	[[Category: De Rosa M]]
-	~~[[Category: Amyloidosis]]~~	+
-	~~[[Category: Beta-sandwitch]]~~	+
-	~~[[Category: Genetic disease]]~~	+
-	~~[[Category: Immune system]]~~	+
-	~~[[Category: Immunoglobin]]~~	+
-	~~[[Category: Mhc class i]]~~	+
-	~~[[Category: Pathologic mutation~~]]	+

OCA at 10:12, 1 May 2019

OCA — Wed, 01 May 2019 10:12:56 GMT

←Older revision		Revision as of 10:12, 1 May 2019
Line 1:		Line 1:
		+
	==Crystal structure of the D53N Beta-2 Microglobulin mutant==		==Crystal structure of the D53N Beta-2 Microglobulin mutant==
-	<StructureSection load='4rms' size='340' side='right' caption='[[4rms]], [[Resolution\|resolution]] 1.70Å' scene=''>	+	<StructureSection load='4rms' size='340' side='right'caption='[[4rms]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4rms]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RMS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RMS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4rms]] is a 1 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=4RMS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RMS FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2yxf\|2yxf]], [[4fxl\|4fxl]], [[4rmq\|4rmq]], [[4rmr\|4rmr]], [[4rmt\|4rmt]], [[4rmu\|4rmu]], [[4rmv\|4rmv]], [[4rmw\|4rmw]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2yxf\|2yxf]], [[4fxl\|4fxl]], [[4rmq\|4rmq]], [[4rmr\|4rmr]], [[4rmt\|4rmt]], [[4rmu\|4rmu]], [[4rmv\|4rmv]], [[4rmw\|4rmw]]</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=4rms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rms OCA], [http://pdbe.org/4rms PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rms RCSB], [http://www.ebi.ac.uk/pdbsum/4rms PDBsum]</span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B2M, CDABP0092, HDCMA22P, NM_004048 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4rms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rms OCA], [http://pdbe.org/4rms PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rms RCSB], [http://www.ebi.ac.uk/pdbsum/4rms PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rms ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 22:
	</div>		</div>
	<div class="pdbe-citations 4rms" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4rms" 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: Human]]
		+	[[Category: Large Structures]]
	[[Category: Bolognesi, M]]		[[Category: Bolognesi, M]]
	[[Category: Ricagno, S]]		[[Category: Ricagno, S]]

OCA at 07:16, 9 December 2015

OCA — Wed, 09 Dec 2015 07:16:40 GMT

←Older revision		Revision as of 07:16, 9 December 2015
Line 11:		Line 11:
	== 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.		[[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 ==
		+	D76N is the first natural variant of human beta-2 microglobulin (beta2m) so far identified. Contrary to the wt protein, this mutant readily forms amyloid fibres in physiological conditions, leading to a systemic and severe amyloidosis. Although the Asp76Asn mutant has been extensively characterized, the molecular bases of its instability and aggregation propensity remain elusive. In this work all Asp residues of human beta2m were individually substituted to Asn; D-to-N mutants (D34N, D38N, D53N, D59N, D96N and D98N) were characterised in terms of thermodynamic stability and aggregation propensity. Moreover, crystal structures of the D38N, D53N, D59N and D98N variants were solved at high-resolution (1.24-1.70 A). Despite showing some significant variations in their thermal stabilities, none showed the dramatic drop in melting temperature (relative to the wt protein) as observed for the pathogenic mutant. Consistently, none of the variants here described displayed any increase in aggregation propensity under the experimental conditions tested. The crystal structures confirmed that D-to-N mutations are generally well tolerated, and lead only to minor reorganization of the side chains in close proximity of the mutated residue. D38N is the only exception, where backbone readjustments and a redistribution of the surface electrostatic charges are observed. Overall, our results suggest that neither removing negative charges at sites 34, 38, 53, 59, 96 and 98, nor the difference in beta2m pI, are the cause of the aggressive phenotype observed in D76N. We propose that the dramatic effects of the D76N natural mutation must be linked to effects related to the crucial location of this residue within the beta2m fold.
		+
		+	Decoding the Structural Bases of D76N ss2-Microglobulin High Amyloidogenicity through Crystallography and Asn-Scan Mutagenesis.,de Rosa M, Barbiroli A, Giorgetti S, Mangione PP, Bolognesi M, Ricagno S PLoS One. 2015 Dec 1;10(12):e0144061. doi: 10.1371/journal.pone.0144061., eCollection 2015. PMID:26625273<ref>PMID:26625273</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4rms" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:54, 1 December 2015

OCA — Tue, 01 Dec 2015 18:54:52 GMT

←Older revision		Revision as of 18:54, 1 December 2015
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of the D53N Beta-2 Microglobulin mutant==
-		+	<StructureSection load='4rms' size='340' side='right' caption='[[4rms]], [[Resolution\|resolution]] 1.70Å' scene=''>
-	~~The entry~~ 4rms is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4rms]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RMS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RMS FirstGlance]. <br>
-	~~Authors~~: ~~de Rosa~~, M., ~~Bolognesi~~, M., ~~Ricagno~~, S.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
-		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2yxf\|2yxf]], [[4fxl\|4fxl]], [[4rmq\|4rmq]], [[4rmr\|4rmr]], [[4rmt\|4rmt]], [[4rmu\|4rmu]], [[4rmv\|4rmv]], [[4rmw\|4rmw]]</td></tr>
-	~~Description: Crystal structure of the D53N Beta-2 Microglobulin mutant~~	+	<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=4rms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rms OCA], [http://pdbe.org/4rms PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rms RCSB], [http://www.ebi.ac.uk/pdbsum/4rms PDBsum]</span></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	</table>
-	[[~~Category~~: ~~Ricagno, S~~]]	+	== Disease ==
-	[[~~Category~~: ~~De Rosa, M~~]]	+	[[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.
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Bolognesi, M]]		[[Category: Bolognesi, M]]
		+	[[Category: Ricagno, S]]
		+	[[Category: Rosa, M de]]
		+	[[Category: Amyloidosis]]
		+	[[Category: Beta-sandwitch]]
		+	[[Category: Genetic disease]]
		+	[[Category: Immune system]]
		+	[[Category: Immunoglobin]]
		+	[[Category: Mhc class i]]
		+	[[Category: Pathologic mutation]]

OCA at 17:04, 24 December 2014

OCA — Wed, 24 Dec 2014 17:04:18 GMT

←Older revision		Revision as of 17:04, 24 December 2014
Line 6:		Line 6:

	Description: Crystal structure of the D53N Beta-2 Microglobulin mutant		Description: Crystal structure of the D53N Beta-2 Microglobulin mutant
		+	[[Category: Unreleased Structures]]
		+	[[Category: Ricagno, S]]
		+	[[Category: De Rosa, M]]
		+	[[Category: Bolognesi, M]]

OCA at 07:39, 5 November 2014

OCA — Wed, 05 Nov 2014 07:39:50 GMT

←Older revision		Revision as of 07:39, 5 November 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4rms is ON HOLD	+	The entry 4rms is ON HOLD until Paper Publication

	Authors: de Rosa, M., Bolognesi, M., Ricagno, S.		Authors: de Rosa, M., Bolognesi, M., Ricagno, S.

	Description: Crystal structure of the D53N Beta-2 Microglobulin mutant		Description: Crystal structure of the D53N Beta-2 Microglobulin mutant

OCA: Protected "4rms" [edit=sysop:move=sysop]

OCA — Wed, 29 Oct 2014 10:10:14 GMT

Protected "4rms" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:10, 29 October 2014

OCA: New page: '''Unreleased structure''' The entry 4rms is ON HOLD Authors: de Rosa, M., Bolognesi, M., Ricagno, S. Description: Crystal structure of the D53N Beta-2 Microglobulin mutant

OCA — Wed, 29 Oct 2014 10:10:13 GMT

New page: '''Unreleased structure''' The entry 4rms is ON HOLD Authors: de Rosa, M., Bolognesi, M., Ricagno, S. Description: Crystal structure of the D53N Beta-2 Microglobulin mutant

New page

'''Unreleased structure'''

The entry 4rms is ON HOLD

Authors: de Rosa, M., Bolognesi, M., Ricagno, S.

Description: Crystal structure of the D53N Beta-2 Microglobulin mutant