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3bwa
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3bwa]] is a 3 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=3BWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BWA FirstGlance]. <br> | <table><tr><td colspan='2'>[[3bwa]] is a 3 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=3BWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BWA FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bw9|3bw9]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bw9|3bw9]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bwa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3bwa RCSB], [http://www.ebi.ac.uk/pdbsum/3bwa 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=3bwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bwa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3bwa RCSB], [http://www.ebi.ac.uk/pdbsum/3bwa PDBsum]</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> | [[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> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Archbold, J K | + | [[Category: Archbold, J K]] |
| - | [[Category: Burrows, S R | + | [[Category: Burrows, S R]] |
| - | [[Category: Cooper, L | + | [[Category: Cooper, L]] |
| - | [[Category: Gras, S | + | [[Category: Gras, S]] |
| - | [[Category: Khanna, R | + | [[Category: Khanna, R]] |
| - | [[Category: Marland, Z | + | [[Category: Marland, Z]] |
| - | [[Category: McCluskey, J | + | [[Category: McCluskey, J]] |
| - | [[Category: Miles, J J | + | [[Category: Miles, J J]] |
| - | [[Category: Rossjohn, J | + | [[Category: Rossjohn, J]] |
| - | [[Category: Silins, S L | + | [[Category: Silins, S L]] |
| - | [[Category: Tynan, F E | + | [[Category: Tynan, F E]] |
| - | [[Category: Wynn, K K | + | [[Category: Wynn, K K]] |
[[Category: Disease mutation]] | [[Category: Disease mutation]] | ||
[[Category: Glycation]] | [[Category: Glycation]] | ||
Revision as of 08:06, 20 January 2015
Crystal Structure of HLA B*3508 in complex with a HCMV 8-mer peptide from the pp65 protein
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Categories: Homo sapiens | Archbold, J K | Burrows, S R | Cooper, L | Gras, S | Khanna, R | Marland, Z | McCluskey, J | Miles, J J | Rossjohn, J | Silins, S L | Tynan, F E | Wynn, K K | Disease mutation | Glycation | Glycoprotein | Hcmv | Hla b*3508 | Host-virus interaction | Immune response | Immune system | Immunoglobulin domain | Immunology | Membrane | Mhc i | Phosphoprotein | Pp65 | Pyrrolidone carboxylic acid | Secreted | Tegument protein | Transmembrane | Viral matrix protein | Virion

