7dyn: Difference between revisions
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<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> | <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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == 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. | 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> | 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> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Latest revision as of 11:40, 17 October 2024
Phosphorylation of MHC I peptidePhosphorylation of MHC I peptide
Structural highlights
Publication 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. See AlsoReferences
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