7dyn: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==== | ==Phosphorylation of MHC I peptide== | ||
<StructureSection load='7dyn' size='340' side='right'caption='[[7dyn]]' scene=''> | <StructureSection load='7dyn' size='340' side='right'caption='[[7dyn]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7dyn]] 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=7DYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DYN FirstGlance]. <br> | ||
</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=7dyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dyn OCA], [https://pdbe.org/7dyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dyn RCSB], [https://www.ebi.ac.uk/pdbsum/7dyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dyn ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=7dyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dyn OCA], [https://pdbe.org/7dyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dyn RCSB], [https://www.ebi.ac.uk/pdbsum/7dyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dyn ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/O78189_HUMAN O78189_HUMAN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Phosphopeptides presented by major histocompatibility complex (MHC) class I have been regarded as a pivotal type of cancer neoantigens that are recognized by T cells. The structural basis of single-phosphorylated peptide presentation has been well studied. Diphosphorylation with one interval between two sites is one of the prevalent forms of multisite-phosphorylated peptides. Herein, we determined the molecular basis of presentation of two P4/P6 double pS-containing peptides by HLA-B27 and compared them with unmodified and single-phosphorylated peptide complexes. These data clarified not only the HLA allele-specific presentation of phosphopeptides by MHC class I molecules but also the cooperativity of peptide conformation within P4 and P6 phosphorylation sites. The phosphorylation of P6 site can influence the binding mode of P4 phosphorylated site to HLA-B27. And we found the diphospho-dependent attenuated effect of peptide binding affinity. This study provides insights into the MHC presentation features of diphosphopeptides, which is different from monophosphopeptides. | |||
Phosphosite-dependent presentation of dual phosphorylated peptides by MHC class I molecules.,Zhao Y, Sun M, Zhang N, Liu X, Yue C, Feng L, Ji S, Liu X, Qi J, Wong CCL, Gao GF, Liu WJ iScience. 2022 Mar 1;25(4):104013. doi: 10.1016/j.isci.2022.104013. eCollection, 2022 Apr 15. PMID:35310951<ref>PMID:35310951</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7dyn" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Feng L]] | ||
[[Category: Liu WJ]] | |||
[[Category: Qi JX]] | |||
[[Category: Sun MW]] | |||
Revision as of 09:21, 26 October 2022
Phosphorylation of MHC I peptidePhosphorylation of MHC I peptide
Structural highlights
FunctionPublication Abstract from PubMedPhosphopeptides presented by major histocompatibility complex (MHC) class I have been regarded as a pivotal type of cancer neoantigens that are recognized by T cells. The structural basis of single-phosphorylated peptide presentation has been well studied. Diphosphorylation with one interval between two sites is one of the prevalent forms of multisite-phosphorylated peptides. Herein, we determined the molecular basis of presentation of two P4/P6 double pS-containing peptides by HLA-B27 and compared them with unmodified and single-phosphorylated peptide complexes. These data clarified not only the HLA allele-specific presentation of phosphopeptides by MHC class I molecules but also the cooperativity of peptide conformation within P4 and P6 phosphorylation sites. The phosphorylation of P6 site can influence the binding mode of P4 phosphorylated site to HLA-B27. And we found the diphospho-dependent attenuated effect of peptide binding affinity. This study provides insights into the MHC presentation features of diphosphopeptides, which is different from monophosphopeptides. Phosphosite-dependent presentation of dual phosphorylated peptides by MHC class I molecules.,Zhao Y, Sun M, Zhang N, Liu X, Yue C, Feng L, Ji S, Liu X, Qi J, Wong CCL, Gao GF, Liu WJ iScience. 2022 Mar 1;25(4):104013. doi: 10.1016/j.isci.2022.104013. eCollection, 2022 Apr 15. PMID:35310951[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||