8tq7: Difference between revisions
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==Crystal structure of Fab.34.2.12 in complex with MHC-I (H2-Dd)== | |||
<StructureSection load='8tq7' size='340' side='right'caption='[[8tq7]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8tq7]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/HIV-1_M:B_HXB2R HIV-1 M:B_HXB2R] 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=8TQ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8TQ7 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]] 2.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=8tq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8tq7 OCA], [https://pdbe.org/8tq7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8tq7 RCSB], [https://www.ebi.ac.uk/pdbsum/8tq7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8tq7 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 == | |||
mAbs to MHC class I (MHC-I) molecules have proved to be crucial reagents for tissue typing and fundamental studies of immune recognition. To augment our understanding of epitopic sites seen by a set of anti-MHC-I mAb, we determined X-ray crystal structures of four complexes of anti-MHC-I Fabs bound to peptide/MHC-I/beta2-microglobulin (pMHC-I). An anti-H2-Dd mAb, two anti-MHC-I alpha3 domain mAbs, and an anti-beta2-microglobulin mAb bind pMHC-I at sites consistent with earlier mutational and functional experiments, and the structures explain allelomorph specificity. Comparison of the experimentally determined structures with computationally derived models using AlphaFold Multimer showed that although predictions of the individual pMHC-I heterodimers were quite acceptable, the computational models failed to properly identify the docking sites of the mAb on pMHC-I. The experimental and predicted structures provide insight into strengths and weaknesses of purely computational approaches and suggest areas that merit additional attention. | |||
Experimental Structures of Antibody/MHC-I Complexes Reveal Details of Epitopes Overlooked by Computational Prediction.,Boyd LF, Jiang J, Ahmad J, Natarajan K, Margulies DH J Immunol. 2024 Apr 15;212(8):1366-1380. doi: 10.4049/jimmunol.2300839. PMID:38456672<ref>PMID:38456672</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8tq7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: HIV-1 M:B_HXB2R]] | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Boyd LF]] | |||
[[Category: Jiang J]] | |||
[[Category: Margulies DH]] | |||
[[Category: Natarajan K]] | |||
Latest revision as of 15:11, 30 October 2024
Crystal structure of Fab.34.2.12 in complex with MHC-I (H2-Dd)Crystal structure of Fab.34.2.12 in complex with MHC-I (H2-Dd)
Structural highlights
FunctionHA12_MOUSE Involved in the presentation of foreign antigens to the immune system. Publication Abstract from PubMedmAbs to MHC class I (MHC-I) molecules have proved to be crucial reagents for tissue typing and fundamental studies of immune recognition. To augment our understanding of epitopic sites seen by a set of anti-MHC-I mAb, we determined X-ray crystal structures of four complexes of anti-MHC-I Fabs bound to peptide/MHC-I/beta2-microglobulin (pMHC-I). An anti-H2-Dd mAb, two anti-MHC-I alpha3 domain mAbs, and an anti-beta2-microglobulin mAb bind pMHC-I at sites consistent with earlier mutational and functional experiments, and the structures explain allelomorph specificity. Comparison of the experimentally determined structures with computationally derived models using AlphaFold Multimer showed that although predictions of the individual pMHC-I heterodimers were quite acceptable, the computational models failed to properly identify the docking sites of the mAb on pMHC-I. The experimental and predicted structures provide insight into strengths and weaknesses of purely computational approaches and suggest areas that merit additional attention. Experimental Structures of Antibody/MHC-I Complexes Reveal Details of Epitopes Overlooked by Computational Prediction.,Boyd LF, Jiang J, Ahmad J, Natarajan K, Margulies DH J Immunol. 2024 Apr 15;212(8):1366-1380. doi: 10.4049/jimmunol.2300839. PMID:38456672[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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