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| | ==Structure of a monoclonal antibody complexed with its MHC-I antigen== | | ==Structure of a monoclonal antibody complexed with its MHC-I antigen== |
| - | <StructureSection load='3v4u' size='340' side='right' caption='[[3v4u]], [[Resolution|resolution]] 1.64Å' scene=''> | + | <StructureSection load='3v4u' size='340' side='right'caption='[[3v4u]], [[Resolution|resolution]] 1.64Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3v4u]] is a 3 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3uo1|3uo1]], [[3uyr|3uyr]], [[3v52|3v52]]</td></tr> | + | </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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3v4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v4u OCA], [http://pdbe.org/3v4u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3v4u RCSB], [http://www.ebi.ac.uk/pdbsum/3v4u PDBsum], [http://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 == |
| - | [[http://www.uniprot.org/uniprot/HA1L_MOUSE HA1L_MOUSE]] Involved in the presentation of foreign antigens to the immune system. | + | [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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| | ==See Also== | | ==See Also== |
| - | *[[3D structures of monoclonal antibody|3D structures of monoclonal antibody]] | + | *[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| - | [[Category: Mage, M G]] | + | [[Category: Mage MG]] |
| - | [[Category: Margulies, D H]] | + | [[Category: Margulies DH]] |
| - | [[Category: Natarajan, K]] | + | [[Category: Natarajan K]] |
| - | [[Category: Wang, R]] | + | [[Category: Wang R]] |
| - | [[Category: 3-10 helix]]
| + | |
| - | [[Category: Ig-fold]]
| + | |
| - | [[Category: Immune system]]
| + | |
| Structural highlights
Function
A2NHM3_MOUSE
Publication Abstract from PubMed
MHC 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 Also
References
- ↑ Mage MG, Dolan MA, Wang R, Boyd LF, Revilleza MJ, Robinson H, Natarajan K, Myers NB, Hansen TH, Margulies DH. The Peptide-receptive transition state of MHC class I molecules: insight from structure and molecular dynamics. J Immunol. 2012 Aug 1;189(3):1391-9. Epub 2012 Jun 29. PMID:22753930 doi:10.4049/jimmunol.1200831
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