5nn5 - Revision history

OCA at 13:10, 15 November 2023

OCA — Wed, 15 Nov 2023 13:10:20 GMT

←Older revision		Revision as of 13:10, 15 November 2023
Line 1:		Line 1:

	==Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with 1-deoxynojirimycin==		==Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with 1-deoxynojirimycin==
-	<StructureSection load='5nn5' size='340' side='right' caption='[[5nn5]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='5nn5' size='340' side='right'caption='[[5nn5]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5nn5]] 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=5NN5 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5NN5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5nn5]] 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=5NN5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NN5 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NOJ:1-DEOXYNOJIRIMYCIN'>NOJ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2Å</td></tr>
-	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NOJ:1-DEOXYNOJIRIMYCIN'>NOJ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5nn3\|5nn3]], [[5nn4\|5nn4]]</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=5nn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nn5 OCA], [https://pdbe.org/5nn5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nn5 RCSB], [https://www.ebi.ac.uk/pdbsum/5nn5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nn5 ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GAA ([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/Alpha-glucosidase Alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20] </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=5nn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nn5 OCA], [~~http~~://pdbe.org/5nn5 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5nn5 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5nn5 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5nn5 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/LYAG_HUMAN LYAG_HUMAN]] Glycogen storage disease due to acid maltase deficiency, infantile onset;Glycogen storage disease due to acid maltase deficiency, juvenile onset;Glycogen storage disease due to acid maltase deficiency, adult onset. The disease is caused by mutations affecting the gene represented in this entry.	+	[https://www.uniprot.org/uniprot/LYAG_HUMAN LYAG_HUMAN] Glycogen storage disease due to acid maltase deficiency, infantile onset;Glycogen storage disease due to acid maltase deficiency, juvenile onset;Glycogen storage disease due to acid maltase deficiency, adult onset. The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/LYAG_HUMAN LYAG_HUMAN]] Essential for the degradation of glygogen to glucose in lysosomes.	+	[https://www.uniprot.org/uniprot/LYAG_HUMAN LYAG_HUMAN] Essential for the degradation of glygogen to glucose in lysosomes.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 5nn5" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5nn5" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Alpha-glucosidase 3D structures\|Alpha-glucosidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Alpha-glucosidase~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Human~~]]	+	[[Category: Large Structures]]
-	[[Category: Bourne, Y]]	+	[[Category: Bourne Y]]
-	[[Category: Cobucci-Ponzano, B]]	+	[[Category: Cobucci-Ponzano B]]
-	[[Category: Ferrara~~, M C~~]]	+	[[Category: Ferrara MC]]
-	[[Category: Germany, S]]	+	[[Category: Germany S]]
-	[[Category: Iacono, R]]	+	[[Category: Iacono R]]
-	[[Category: Moracci, M]]	+	[[Category: Moracci M]]
-	[[Category: Parenti, G]]	+	[[Category: Parenti G]]
-	[[Category: Roig-Zamboni, V]]	+	[[Category: Roig-Zamboni V]]
-	~~[[Category: Glycogen catabolism]]~~	+
-	~~[[Category: Glycoside hydrolase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Lysosome]]~~	+
-	~~[[Category: Pompe disease~~]]	+

OCA at 06:17, 1 November 2017

OCA — Wed, 01 Nov 2017 06:17:44 GMT

←Older revision		Revision as of 06:17, 1 November 2017
Line 3:		Line 3:
	<StructureSection load='5nn5' size='340' side='right' caption='[[5nn5]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='5nn5' size='340' side='right' caption='[[5nn5]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5nn5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NN5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NN5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5nn5]] 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=5NN5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NN5 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NOJ:1-DEOXYNOJIRIMYCIN'>NOJ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NOJ:1-DEOXYNOJIRIMYCIN'>NOJ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5nn3\|5nn3]], [[5nn4\|5nn4]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5nn3\|5nn3]], [[5nn4\|5nn4]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GAA ([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/Alpha-glucosidase Alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-glucosidase Alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20] </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=5nn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nn5 OCA], [http://pdbe.org/5nn5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nn5 RCSB], [http://www.ebi.ac.uk/pdbsum/5nn5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nn5 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=5nn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nn5 OCA], [http://pdbe.org/5nn5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nn5 RCSB], [http://www.ebi.ac.uk/pdbsum/5nn5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nn5 ProSAT]</span></td></tr>
Line 14:		Line 15:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/LYAG_HUMAN LYAG_HUMAN]] Essential for the degradation of glygogen to glucose in lysosomes.		[[http://www.uniprot.org/uniprot/LYAG_HUMAN LYAG_HUMAN]] Essential for the degradation of glygogen to glucose in lysosomes.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid alpha-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death. Numerous disease-causing mutations in the gaa gene have been reported, but the structural effects of the pathological variants were unknown. Here we present the high-resolution crystal structures of recombinant human GAA (rhGAA), the standard care of Pompe disease. These structures portray the unbound form of rhGAA and complexes thereof with active site-directed inhibitors, providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations. Furthermore, we report the structure of rhGAA in complex with the allosteric pharmacological chaperone N-acetylcysteine, which reveals the stabilizing function of this chaperone at the structural level.
		+
		+	Structure of human lysosomal acid alpha-glucosidase-a guide for the treatment of Pompe disease.,Roig-Zamboni V, Cobucci-Ponzano B, Iacono R, Ferrara MC, Germany S, Bourne Y, Parenti G, Moracci M, Sulzenbacher G Nat Commun. 2017 Oct 24;8(1):1111. doi: 10.1038/s41467-017-01263-3. PMID:29061980<ref>PMID:29061980</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5nn5" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Alpha-glucosidase]]		[[Category: Alpha-glucosidase]]
		+	[[Category: Human]]
	[[Category: Bourne, Y]]		[[Category: Bourne, Y]]
	[[Category: Cobucci-Ponzano, B]]		[[Category: Cobucci-Ponzano, B]]

OCA at 07:13, 25 October 2017

OCA — Wed, 25 Oct 2017 07:13:02 GMT

←Older revision		Revision as of 07:13, 25 October 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5nn5 ~~is ON HOLD until Paper Publication~~	+	==Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with 1-deoxynojirimycin==
-		+	<StructureSection load='5nn5' size='340' side='right' caption='[[5nn5]], [[Resolution\|resolution]] 2.00Å' scene=''>
-	~~Authors~~: ~~Roig~~-~~Zamboni, V~~., ~~Cobucci~~-~~Ponzano~~, B., ~~Iacono~~, R., ~~Ferrara~~, M.C., ~~Germany~~, S., ~~Parenti~~, G., ~~Bourne~~, Y., ~~Moracci~~, M.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5nn5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NN5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NN5 FirstGlance]. <br>
-	~~Description~~: ~~Crystal structure~~ of ~~human lysosomal acid-alpha~~-glucosidase, ~~GAA, in complex with 1~~-~~deoxynojirimycin~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NOJ:1-DEOXYNOJIRIMYCIN'>NOJ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5nn3\|5nn3]], [[5nn4\|5nn4]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-glucosidase Alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20] </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=5nn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nn5 OCA], [http://pdbe.org/5nn5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nn5 RCSB], [http://www.ebi.ac.uk/pdbsum/5nn5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nn5 ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/LYAG_HUMAN LYAG_HUMAN]] Glycogen storage disease due to acid maltase deficiency, infantile onset;Glycogen storage disease due to acid maltase deficiency, juvenile onset;Glycogen storage disease due to acid maltase deficiency, adult onset. The disease is caused by mutations affecting the gene represented in this entry.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/LYAG_HUMAN LYAG_HUMAN]] Essential for the degradation of glygogen to glucose in lysosomes.
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Alpha-glucosidase]]
		+	[[Category: Bourne, Y]]
		+	[[Category: Cobucci-Ponzano, B]]
		+	[[Category: Ferrara, M C]]
	[[Category: Germany, S]]		[[Category: Germany, S]]
-	[[Category: Ferrara, M.C]]
	[[Category: Iacono, R]]		[[Category: Iacono, R]]
		+	[[Category: Moracci, M]]
		+	[[Category: Parenti, G]]
	[[Category: Roig-Zamboni, V]]		[[Category: Roig-Zamboni, V]]
-	[[Category: ~~Parenti, G~~]]	+	[[Category: Glycogen catabolism]]
-	[[Category: ~~Bourne, Y~~]]	+	[[Category: Glycoside hydrolase]]
-	[[Category: ~~Cobucci-Ponzano, B~~]]	+	[[Category: Hydrolase]]
-	[[Category: ~~Moracci, M~~]]	+	[[Category: Lysosome]]
		+	[[Category: Pompe disease]]

OCA: Protected "5nn5" [edit=sysop:move=sysop]

OCA — Wed, 19 Apr 2017 09:41:03 GMT

Protected "5nn5" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:41, 19 April 2017

OCA: New page: '''Unreleased structure''' The entry 5nn5 is ON HOLD until Paper Publication Authors: Roig-Zamboni, V., Cobucci-Ponzano, B., Iacono, R., Ferrara, M.C., Germany, S., Parenti, G., Bourne,...

OCA — Wed, 19 Apr 2017 09:41:01 GMT

New page: '''Unreleased structure''' The entry 5nn5 is ON HOLD until Paper Publication Authors: Roig-Zamboni, V., Cobucci-Ponzano, B., Iacono, R., Ferrara, M.C., Germany, S., Parenti, G., Bourne,...

New page

'''Unreleased structure'''

The entry 5nn5 is ON HOLD until Paper Publication

Authors: Roig-Zamboni, V., Cobucci-Ponzano, B., Iacono, R., Ferrara, M.C., Germany, S., Parenti, G., Bourne, Y., Moracci, M.

Description: Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with 1-deoxynojirimycin
[[Category: Unreleased Structures]]
[[Category: Germany, S]]
[[Category: Ferrara, M.C]]
[[Category: Iacono, R]]
[[Category: Roig-Zamboni, V]]
[[Category: Parenti, G]]
[[Category: Bourne, Y]]
[[Category: Cobucci-Ponzano, B]]
[[Category: Moracci, M]]