4l29
From Proteopedia
(Difference between revisions)
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{{Large structure}} | {{Large structure}} | ||
- | + | ==Structure of wtMHC class I with NY-ESO1 double mutant== | |
- | + | <StructureSection load='4l29' size='340' side='right' caption='[[4l29]], [[Resolution|resolution]] 3.09Å' scene=''> | |
- | {{ | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[4l29]] is a 42 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=4L29 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L29 FirstGlance]. <br> | |
- | ==Disease== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4l3c|4l3c]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HLA-A, HLAA, HLA_A0201 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), 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=4l29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l29 OCA], [http://pdbe.org/4l29 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4l29 RCSB], [http://www.ebi.ac.uk/pdbsum/4l29 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4l29 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | {{Large structure}} | ||
+ | == 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> | [[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 == | |
- | ==Function== | + | |
[[http://www.uniprot.org/uniprot/1A02_HUMAN 1A02_HUMAN]] Involved in the presentation of foreign 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. | [[http://www.uniprot.org/uniprot/1A02_HUMAN 1A02_HUMAN]] Involved in the presentation of foreign 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 == | ||
+ | To form extracellular aggregates, amyloidogenic proteins bypass the intracellular quality control which normally targets unfolded/aggregated polypeptides. Human D76N beta2-microglobulin (beta2m) variant is the prototype of unstable and amyloidogenic protein which forms abundant extracellular fibrillar deposits. Here we focus on the role of the Class I Major Histocompatibility Complex (MHC) in the intracellular stabilization of D76N beta2m. Using biophysical and structural approaches we show that the MHC containing D76N beta2m (MHC76) displays stability, dissociation patterns and crystal structure comparable to those of the MHC with wild type beta2m. Conversely, limited proteolysis experiments show a reduced protease susceptibility for D76N beta2m within the MHC76 compared to the free variant, suggesting that the MHC has a chaperone-like activity in preventing D76N beta2m degradation within the cell. Accordingly, D76N beta2m is normally assembled in the MHC and circulates as free plasma species in a transgenic mouse model. | ||
- | + | Class I Major Histocomapatibility Complex: the Trojan horse for secretion of amyloidogenic beta2-microglobulin.,Halabelian L, Ricagno S, Giorgetti S, Santambrogio C, Barbiroli A, Pellegrino S, Achour A, Grandori R, Marchese L, Raimondi S, Mangione PP, Esposito G, Al-Shawi R, Simons JP, Speck I, Stoppini M, Bolognesi M, Bellotti V J Biol Chem. 2013 Dec 13. PMID:24338476<ref>PMID:24338476</ref> | |
- | + | ||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 4l29" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Beta-2 microglobulin|Beta-2 microglobulin]] | *[[Beta-2 microglobulin|Beta-2 microglobulin]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
- | [[Category: Bellotti, V | + | </StructureSection> |
- | [[Category: Bolognesi, M | + | [[Category: Human]] |
- | [[Category: Giorgetti, S | + | [[Category: Bellotti, V]] |
- | [[Category: Halabelian, L | + | [[Category: Bolognesi, M]] |
- | [[Category: Ricagno, S | + | [[Category: Giorgetti, S]] |
+ | [[Category: Halabelian, L]] | ||
+ | [[Category: Ricagno, S]] | ||
[[Category: Beta sandwitch]] | [[Category: Beta sandwitch]] | ||
[[Category: Beta-2 microglobulin]] | [[Category: Beta-2 microglobulin]] |
Revision as of 23:25, 4 August 2016
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Structure of wtMHC class I with NY-ESO1 double mutant
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Categories: Human | Bellotti, V | Bolognesi, M | Giorgetti, S | Halabelian, L | Ricagno, S | Beta sandwitch | Beta-2 microglobulin | D76n variant | Hla a0201 | Immune system | Immunglobulin | Mhc | Ny-eso1