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| - | ==Crystal structure of th human lysosome-associated membrane protein LAMP-3 (aka DC-LAMP)== | + | |
| - | <StructureSection load='4akm' size='340' side='right' caption='[[4akm]], [[Resolution|resolution]] 2.69Å' scene=''> | + | ==Crystal structure of the human lysosome-associated membrane protein LAMP-3 (aka DC-LAMP)== |
| | + | <StructureSection load='4akm' size='340' side='right'caption='[[4akm]], [[Resolution|resolution]] 2.69Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4akm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AKM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AKM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4akm]] 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=4AKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AKM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IR3:IRIDIUM+(III)+ION'>IR3</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.687Å</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=4akm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4akm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4akm RCSB], [http://www.ebi.ac.uk/pdbsum/4akm PDBsum]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IR3:IRIDIUM+(III)+ION'>IR3</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4akm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4akm OCA], [https://pdbe.org/4akm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4akm RCSB], [https://www.ebi.ac.uk/pdbsum/4akm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4akm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LAMP3_HUMAN LAMP3_HUMAN]] May play a role in dendritic cell function and in adaptive immunity.<ref>PMID:9768752</ref> | + | [https://www.uniprot.org/uniprot/LAMP3_HUMAN LAMP3_HUMAN] May play a role in dendritic cell function and in adaptive immunity.<ref>PMID:9768752</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | 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 4akm" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Buessow, K]] | + | [[Category: Large Structures]] |
| - | [[Category: Krausze, J]] | + | [[Category: Buessow K]] |
| - | [[Category: Wilke, S]] | + | [[Category: Krausze J]] |
| - | [[Category: Beta prism]] | + | [[Category: Wilke S]] |
| - | [[Category: Glycosylation]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| Structural highlights
Function
LAMP3_HUMAN May play a role in dendritic cell function and in adaptive immunity.[1]
Publication Abstract from PubMed
ABSTRACT: BACKGROUND: The family of lysosome-associated membrane proteins (LAMP) comprises the multifunctional, ubiquitous LAMP-1 and LAMP-2, and the cell type-specific proteins DC-LAMP (LAMP-3), BAD-LAMP (UNC-46, C20orf103) and macrosialin (CD68). LAMPs have been implicated in a multitude of cellular processes, including phagocytosis, autophagy, lipid transport and aging. LAMP-2 isoform A acts as a receptor in chaperone-mediated autophagy. LAMP-2 deficiency causes the fatal Danon disease. The abundant proteins LAMP-1 and LAMP-2 are major constituents of the glycoconjugate coat present on the inside of the lysosomal membrane, the 'lysosomal glycocalyx'. The LAMP family is characterized by a conserved domain of 150 to 200 amino acids with two disulfide bonds. RESULTS: The crystal structure of the conserved domain of human DC-LAMP was solved. It is the first high-resolution structure of a heavily glycosylated lysosomal membrane protein. The structure represents a novel beta-prism fold formed by two beta-sheets bent by beta-bulges and connected by a disulfide bond. Flexible loops and a hydrophobic pocket represent possible sites of molecular interaction. Computational models of the glycosylated luminal regions of LAMP-1 and LAMP-2 indicate that the proteins adopt a compact conformation in close proximity to the lysosomal membrane. The models correspond to the thickness of the lysosomal glycoprotein coat of only 5 to 12 nm, according to electron microscopy. CONCLUSION: The conserved luminal domain of lysosome-associated membrane proteins forms a previously unknown beta-prism fold. Insights into the structure of the lysosomal glycoprotein coat were obtained by computational models of the LAMP-1 and LAMP-2 luminal regions.
Crystal structure of the conserved domain of the DC lysosomal associated membrane protein: implications for the lysosomal glycocalyx.,Wilke S, Krausze J, Bussow K BMC Biol. 2012 Jul 19;10:62. PMID:22809326[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ de Saint-Vis B, Vincent J, Vandenabeele S, Vanbervliet B, Pin JJ, Ait-Yahia S, Patel S, Mattei MG, Banchereau J, Zurawski S, Davoust J, Caux C, Lebecque S. A novel lysosome-associated membrane glycoprotein, DC-LAMP, induced upon DC maturation, is transiently expressed in MHC class II compartment. Immunity. 1998 Sep;9(3):325-36. PMID:9768752
- ↑ Wilke S, Krausze J, Bussow K. Crystal structure of the conserved domain of the DC lysosomal associated membrane protein: implications for the lysosomal glycocalyx. BMC Biol. 2012 Jul 19;10:62. PMID:22809326 doi:10.1186/1741-7007-10-62
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