1jf1: Difference between revisions

New page: left|200px<br /> <applet load="1jf1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jf1, resolution 1.85Å" /> '''Crystal structure o...
 
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[[Image:1jf1.gif|left|200px]]<br />
<applet load="1jf1" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1jf1, resolution 1.85&Aring;" />
'''Crystal structure of HLA-A2*0201 in complex with a decameric altered peptide ligand from the MART-1/Melan-A'''<br />


==Overview==
==Crystal structure of HLA-A2*0201 in complex with a decameric altered peptide ligand from the MART-1/Melan-A==
We have determined high-resolution crystal structures of the complexes of, HLA-A2 molecules with two modified immunodominant peptides from the, melanoma tumor-associated protein Melan-A/Melanoma Ag recognized by T, cells-1. The two peptides, a decamer and nonamer with overlapping, sequences (ELAGIGILTV and ALGIGILTV), are modified in the second residue, to increase their affinity for HLA-A2. The modified decamer is more, immunogenic than the natural peptide and a candidate for peptide-based, melanoma immunotherapy. The crystal structures at 1.8 and 2.15 A, resolution define the differences in binding modes of the modified, peptides, including different clusters of water molecules that appear to, stabilize the peptide-HLA interaction. The structures suggest both how the, wild-type peptides would bind and how three categories of cytotoxic T, lymphocytes with differing fine specificity might recognize the two, peptides.
<StructureSection load='1jf1' size='340' side='right'caption='[[1jf1]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jf1]] 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=1JF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JF1 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]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1jf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jf1 OCA], [https://pdbe.org/1jf1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jf1 RCSB], [https://www.ebi.ac.uk/pdbsum/1jf1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jf1 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/jf/1jf1_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=1jf1 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=142800 142800]], Ankylosing spondylitis, susceptibility to, 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142800 142800]], Hypoproteinemia, hypercatabolic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109700 109700]], Stevens-Johnson syndrome, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142800 142800]]
*[[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]]
1JF1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JF1 OCA].
== References ==
 
<references/>
==Reference==
__TOC__
Crystal structures of two closely related but antigenically distinct HLA-A2/melanocyte-melanoma tumor-antigen peptide complexes., Sliz P, Michielin O, Cerottini JC, Luescher I, Romero P, Karplus M, Wiley DC, J Immunol. 2001 Sep 15;167(6):3276-84. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11544315 11544315]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Cerottini, J.C.]]
[[Category: Cerottini JC]]
[[Category: Karplus, M.]]
[[Category: Karplus M]]
[[Category: Luescher, I.]]
[[Category: Luescher I]]
[[Category: Michielin, O.]]
[[Category: Michielin O]]
[[Category: Romero, P.]]
[[Category: Romero P]]
[[Category: Sliz, P.]]
[[Category: Sliz P]]
[[Category: Wiley, D.C.]]
[[Category: Wiley DC]]
[[Category: ZN]]
[[Category: class i]]
[[Category: human]]
[[Category: melanoma]]
[[Category: melanoma antigen]]
[[Category: mhc]]
[[Category: tumor immunity]]
[[Category: vaccination]]
 
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