1ed3: Difference between revisions
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<StructureSection load='1ed3' size='340' side='right'caption='[[1ed3]], [[Resolution|resolution]] 2.55Å' scene=''> | <StructureSection load='1ed3' size='340' side='right'caption='[[1ed3]], [[Resolution|resolution]] 2.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ed3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1ed3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ED3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ED3 FirstGlance]. <br> | ||
</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=1ed3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ed3 OCA], [https://pdbe.org/1ed3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ed3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ed3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ed3 ProSAT]</span></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]] 2.55Å</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=1ed3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ed3 OCA], [https://pdbe.org/1ed3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ed3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ed3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ed3 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/HA12_RAT HA12_RAT] Involved in the presentation of foreign antigens to the immune system. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | ||
*[[MHC 3D structures|MHC 3D structures]] | *[[MHC 3D structures|MHC 3D structures]] | ||
*[[MHC I 3D structures|MHC I 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Butcher | [[Category: Rattus norvegicus]] | ||
[[Category: Joly | [[Category: Butcher GW]] | ||
[[Category: Speir | [[Category: Joly E]] | ||
[[Category: Stevens | [[Category: Speir JA]] | ||
[[Category: Wilson | [[Category: Stevens J]] | ||
[[Category: Wilson IA]] | |||
Latest revision as of 08:58, 9 August 2023
CRYSTAL STRUCTURE OF RAT MINOR HISTOCOMPATIBILITY ANTIGEN COMPLEX RT1-AA/MTF-E.CRYSTAL STRUCTURE OF RAT MINOR HISTOCOMPATIBILITY ANTIGEN COMPLEX RT1-AA/MTF-E.
Structural highlights
FunctionHA12_RAT Involved in the presentation of foreign antigens to the immune system. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe rat MHC class Ia molecule RT1-Aa has the unusual capacity to bind long peptides ending in arginine, such as MTF-E, a thirteen-residue, maternally transmitted minor histocompatibility antigen. The antigenic structure of MTF-E was unpredictable due to its extraordinary length and two arginines that could serve as potential anchor residues. The crystal structure of RT1-Aa-MTF-E at 2.55 A shows that both peptide termini are anchored, as in other class I molecules, but the central residues in two independent pMHC complexes adopt completely different bulged conformations based on local environment. The MTF-E epitope is fully exposed within the putative T cell receptor (TCR) footprint. The flexibility demonstrated by the MTF-E structures illustrates how different TCRs may be raised against chemically identical, but structurally dissimilar, pMHC complexes. Two different, highly exposed, bulged structures for an unusually long peptide bound to rat MHC class I RT1-Aa.,Speir JA, Stevens J, Joly E, Butcher GW, Wilson IA Immunity. 2001 Jan;14(1):81-92. PMID:11163232[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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