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==Crystal Structure of RTY Phosphopeptide Bound to Human Class I MHC HLA-A2== | ==Crystal Structure of RTY Phosphopeptide Bound to Human Class I MHC HLA-A2== | ||
<StructureSection load='3bh9' size='340' side='right' caption='[[3bh9]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='3bh9' size='340' side='right'caption='[[3bh9]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3bh9]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3bh9]] 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=3BH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BH9 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=3bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bh9 OCA], [https://pdbe.org/3bh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bh9 RCSB], [https://www.ebi.ac.uk/pdbsum/3bh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bh9 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Disease == | == Disease == | ||
[ | [https://www.uniprot.org/uniprot/POF1B_HUMAN POF1B_HUMAN] Defects in POF1B are the cause of premature ovarian failure type 2B (POF2B) [MIM:[https://omim.org/entry/300604 300604]. An ovarian disorder defined as the cessation of ovarian function under the age of 40 years. It is characterized by oligomenorrhea or amenorrhea, in the presence of elevated levels of serum gonadotropins and low estradiol.<ref>PMID:16773570</ref> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/POF1B_HUMAN POF1B_HUMAN] May be involved in ovary development.<ref>PMID:16773570</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/3bh9_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/3bh9_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 33: | Line 31: | ||
</div> | </div> | ||
<div class="pdbe-citations 3bh9" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3bh9" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | |||
*[[MHC 3D structures|MHC 3D structures]] | |||
*[[MHC I 3D structures|MHC I 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Barrett-Wilt | [[Category: Large Structures]] | ||
[[Category: Cobbold | [[Category: Barrett-Wilt GA]] | ||
[[Category: Engelhard | [[Category: Cobbold M]] | ||
[[Category: Hunt | [[Category: Engelhard VH]] | ||
[[Category: Mohammed | [[Category: Hunt DF]] | ||
[[Category: Salim | [[Category: Mohammed F]] | ||
[[Category: Shabanowitz | [[Category: Salim M]] | ||
[[Category: Willcox | [[Category: Shabanowitz J]] | ||
[[Category: Zarling | [[Category: Willcox BE]] | ||
[[Category: Zarling AL]] | |||
Latest revision as of 11:48, 30 October 2024
Crystal Structure of RTY Phosphopeptide Bound to Human Class I MHC HLA-A2Crystal Structure of RTY Phosphopeptide Bound to Human Class I MHC HLA-A2
Structural highlights
DiseasePOF1B_HUMAN Defects in POF1B are the cause of premature ovarian failure type 2B (POF2B) [MIM:300604. An ovarian disorder defined as the cessation of ovarian function under the age of 40 years. It is characterized by oligomenorrhea or amenorrhea, in the presence of elevated levels of serum gonadotropins and low estradiol.[1] FunctionPOF1B_HUMAN May be involved in ovary development.[2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProtein phosphorylation generates a source of phosphopeptides that are presented by major histocompatibility complex class I molecules and recognized by T cells. As deregulated phosphorylation is a hallmark of malignant transformation, the differential display of phosphopeptides on cancer cells provides an immunological signature of 'transformed self'. Here we demonstrate that phosphorylation can considerably increase peptide binding affinity for HLA-A2. To understand this, we solved crystal structures of four phosphopeptide-HLA-A2 complexes. These identified a novel peptide-binding motif centered on a solvent-exposed phosphate anchor. Our findings indicate that deregulated phosphorylation can create neoantigens by promoting binding to major histocompatibility complex molecules or by affecting the antigenic identity of presented epitopes. These results highlight the potential of phosphopeptides as novel targets for cancer immunotherapy. Phosphorylation-dependent interaction between antigenic peptides and MHC class I: a molecular basis for the presentation of transformed self.,Mohammed F, Cobbold M, Zarling AL, Salim M, Barrett-Wilt GA, Shabanowitz J, Hunt DF, Engelhard VH, Willcox BE Nat Immunol. 2008 Nov;9(11):1236-43. Epub 2008 Oct 5. PMID:18836451[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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