5wet: Difference between revisions
New page: '''Unreleased structure''' The entry 5wet is ON HOLD until Paper Publication Authors: Jiang, J.S., Natarajan, K., Boyd, L.F., Margulies, D.H. Description: Crystal Structure of H2-Dd wi... |
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==Crystal Structure of H2-Dd with disulfide-linked 6mer peptide== | |||
<StructureSection load='5wet' size='340' side='right'caption='[[5wet]], [[Resolution|resolution]] 2.64Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5wet]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_(BRU_ISOLATE) Human immunodeficiency virus type 1 (BRU ISOLATE)] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WET 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]] 2.64Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=LEU:LEUCINE'>LEU</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=5wet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wet OCA], [https://pdbe.org/5wet PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wet RCSB], [https://www.ebi.ac.uk/pdbsum/5wet PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wet ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/HA12_MOUSE HA12_MOUSE] Involved in the presentation of foreign antigens to the immune system. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Central to CD8+ T-cell mediated immunity is the recognition of peptide-major histocompatibility complex class I (pMHC-I) proteins displayed by antigen-presenting cells. Chaperone-mediated loading of high-affinity peptides onto MHC-I is a key step in the MHC-I antigen presentation pathway. However, the structure of MHC-I with a chaperone that facilitates peptide loading has not been determined. We report the crystal structure of MHC-I in complex with the peptide editor TAPBPR (TAP binding protein, related), a tapasin homolog. TAPBPR remodels the peptide-binding groove of MHC-I, resulting in the release of low-affinity peptide. Changes include groove relaxation, modifications of key binding pockets, and domain adjustments. This structure captures a peptide-receptive state of MHC-I and provides insights into the mechanism of peptide editing by TAPBPR and, by analogy, tapasin. | |||
Crystal structure of a TAPBPR-MHC-I complex reveals the mechanism of peptide editing in antigen presentation.,Jiang J, Natarajan K, Boyd LF, Morozov GI, Mage MG, Margulies DH Science. 2017 Oct 12. pii: eaao5154. doi: 10.1126/science.aao5154. PMID:29025991<ref>PMID:29025991</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5wet" style="background-color:#fffaf0;"></div> | ||
[[Category: Jiang | |||
[[Category: | ==See Also== | ||
[[Category: Natarajan | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Boyd LF]] | |||
[[Category: Jiang JS]] | |||
[[Category: Margulies DH]] | |||
[[Category: Natarajan K]] | |||
Latest revision as of 13:56, 30 October 2024
Crystal Structure of H2-Dd with disulfide-linked 6mer peptideCrystal Structure of H2-Dd with disulfide-linked 6mer peptide
Structural highlights
FunctionHA12_MOUSE Involved in the presentation of foreign antigens to the immune system. Publication Abstract from PubMedCentral to CD8+ T-cell mediated immunity is the recognition of peptide-major histocompatibility complex class I (pMHC-I) proteins displayed by antigen-presenting cells. Chaperone-mediated loading of high-affinity peptides onto MHC-I is a key step in the MHC-I antigen presentation pathway. However, the structure of MHC-I with a chaperone that facilitates peptide loading has not been determined. We report the crystal structure of MHC-I in complex with the peptide editor TAPBPR (TAP binding protein, related), a tapasin homolog. TAPBPR remodels the peptide-binding groove of MHC-I, resulting in the release of low-affinity peptide. Changes include groove relaxation, modifications of key binding pockets, and domain adjustments. This structure captures a peptide-receptive state of MHC-I and provides insights into the mechanism of peptide editing by TAPBPR and, by analogy, tapasin. Crystal structure of a TAPBPR-MHC-I complex reveals the mechanism of peptide editing in antigen presentation.,Jiang J, Natarajan K, Boyd LF, Morozov GI, Mage MG, Margulies DH Science. 2017 Oct 12. pii: eaao5154. doi: 10.1126/science.aao5154. PMID:29025991[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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