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New page: left|200px<br /> <applet load="1m6o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m6o, resolution 1.6Å" /> '''Crystal Structure of...
 
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[[Image:1m6o.gif|left|200px]]<br />
<applet load="1m6o" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1m6o, resolution 1.6&Aring;" />
'''Crystal Structure of HLA B*4402 in complex with HLA DPA*0201 peptide'''<br />


==Overview==
==Crystal Structure of HLA B*4402 in complex with HLA DPA*0201 peptide==
HLA-B*4402 and B*4403 are naturally occurring MHC class I alleles that are, both found at a high frequency in all human populations, and yet they only, differ by one residue on the alpha2 helix (B*4402 Asp156--&gt;B*4403 Leu156)., CTLs discriminate between HLA-B*4402 and B*4403, and these allotypes, stimulate strong mutual allogeneic responses reflecting their known, barrier to hemopoeitic stem cell transplantation. Although HLA-B*4402 and, B*4403 share &gt;95% of their peptide repertoire, B*4403 presents more unique, peptides than B*4402, consistent with the stronger T cell alloreactivity, observed toward B*4403 compared with B*4402. Crystal structures of B*4402, and B*4403 show how the polymorphism at position 156 is completely buried, and yet alters both the peptide and the heavy chain conformation, relaxing, ligand selection by B*4403 compared with B*4402. Thus, the polymorphism, between HLA-B*4402 and B*4403 modifies both peptide repertoire and T cell, recognition, and is reflected in the paradoxically powerful alloreactivity, that occurs across this "minimal" mismatch. The findings suggest that, these closely related class I genes are maintained in diverse human, populations through their differential impact on the selection of peptide, ligands and the T cell repertoire.
<StructureSection load='1m6o' size='340' side='right'caption='[[1m6o]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1m6o]] is a 3 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=1M6O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M6O FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</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=1m6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m6o OCA], [https://pdbe.org/1m6o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m6o RCSB], [https://www.ebi.ac.uk/pdbsum/1m6o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m6o ProSAT]</span></td></tr>
</table>
== Disease ==
[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 ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m6/1m6o_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m6o ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142830 142830]], Hypoproteinemia, hypercatabolic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109700 109700]], Spondyloarthropathy, susceptibility to, 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142830 142830]], Stevens-Johnson syndrome, carbamazepine-induced, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142830 142830]]
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
 
*[[MHC 3D structures|MHC 3D structures]]
==About this Structure==
*[[MHC I 3D structures|MHC I 3D structures]]
1M6O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M6O OCA].
== References ==
 
<references/>
==Reference==
__TOC__
A naturally selected dimorphism within the HLA-B44 supertype alters class I structure, peptide repertoire, and T cell recognition., Macdonald WA, Purcell AW, Mifsud NA, Ely LK, Williams DS, Chang L, Gorman JJ, Clements CS, Kjer-Nielsen L, Koelle DM, Burrows SR, Tait BD, Holdsworth R, Brooks AG, Lovrecz GO, Lu L, Rossjohn J, McCluskey J, J Exp Med. 2003 Sep 1;198(5):679-91. Epub 2003 Aug 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12939341 12939341]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Brooks, A.G.]]
[[Category: Brooks AG]]
[[Category: Clements, C.S.]]
[[Category: Clements CS]]
[[Category: Ely, L.K.]]
[[Category: Ely LK]]
[[Category: Gorman, J.J.]]
[[Category: Gorman JJ]]
[[Category: Kjer-Nielsen, L.]]
[[Category: Kjer-Nielsen L]]
[[Category: Koelle, D.M.]]
[[Category: Koelle DM]]
[[Category: Lovrecz, G.O.]]
[[Category: Lovrecz GO]]
[[Category: Lu, L.]]
[[Category: Lu L]]
[[Category: Macdonald, W.A.]]
[[Category: Macdonald WA]]
[[Category: McCluskey, J.]]
[[Category: McCluskey J]]
[[Category: Mifsud, N.A.]]
[[Category: Mifsud NA]]
[[Category: Purcell, A.W.]]
[[Category: Purcell AW]]
[[Category: Rossjohn, J.]]
[[Category: Rossjohn J]]
[[Category: Williams, D.S.]]
[[Category: Williams DS]]
[[Category: glycoprotein]]
[[Category: mhc i]]
[[Category: signal]]
 
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