3v4u: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3v4u]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V4U FirstGlance]. <br> | <table><tr><td colspan='2'>[[3v4u]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V4U 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]] 1.64Å</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=3v4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v4u OCA], [https://pdbe.org/3v4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v4u RCSB], [https://www.ebi.ac.uk/pdbsum/3v4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v4u 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=3v4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v4u OCA], [https://pdbe.org/3v4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v4u RCSB], [https://www.ebi.ac.uk/pdbsum/3v4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v4u ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/A2NHM3_MOUSE A2NHM3_MOUSE] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Mage | [[Category: Mage MG]] | ||
[[Category: Margulies | [[Category: Margulies DH]] | ||
[[Category: Natarajan | [[Category: Natarajan K]] | ||
[[Category: Wang | [[Category: Wang R]] | ||
Latest revision as of 12:47, 30 October 2024
Structure of a monoclonal antibody complexed with its MHC-I antigenStructure of a monoclonal antibody complexed with its MHC-I antigen
Structural highlights
FunctionPublication Abstract from PubMedMHC class I (MHC-I) proteins of the adaptive immune system require antigenic peptides for maintenance of mature conformation and immune function via specific recognition by MHC-I-restricted CD8(+) T lymphocytes. New MHC-I molecules in the endoplasmic reticulum are held by chaperones in a peptide-receptive (PR) transition state pending release by tightly binding peptides. In this study, we show, by crystallographic, docking, and molecular dynamics methods, dramatic movement of a hinged unit containing a conserved 3(10) helix that flips from an exposed "open" position in the PR transition state to a "closed" position with buried hydrophobic side chains in the peptide-loaded mature molecule. Crystallography of hinged unit residues 46-53 of murine H-2L(d) MHC-I H chain, complexed with mAb 64-3-7, demonstrates solvent exposure of these residues in the PR conformation. Docking and molecular dynamics predict how this segment moves to help form the A and B pockets crucial for the tight peptide binding needed for stability of the mature peptide-loaded conformation, chaperone dissociation, and Ag presentation. The Peptide-receptive transition state of MHC class I molecules: insight from structure and molecular dynamics.,Mage MG, Dolan MA, Wang R, Boyd LF, Revilleza MJ, Robinson H, Natarajan K, Myers NB, Hansen TH, Margulies DH J Immunol. 2012 Aug 1;189(3):1391-9. Epub 2012 Jun 29. PMID:22753930[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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