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| | <StructureSection load='1kjv' size='340' side='right'caption='[[1kjv]], [[Resolution|resolution]] 1.48Å' scene=''> | | <StructureSection load='1kjv' size='340' side='right'caption='[[1kjv]], [[Resolution|resolution]] 1.48Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1kjv]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KJV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KJV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1kjv]] is a 3 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=1KJV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KJV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.48Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ed3|1ed3]], [[1kjm|1kjm]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1kjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kjv OCA], [https://pdbe.org/1kjv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kjv RCSB], [https://www.ebi.ac.uk/pdbsum/1kjv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kjv 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=1kjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kjv OCA], [https://pdbe.org/1kjv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kjv RCSB], [https://www.ebi.ac.uk/pdbsum/1kjv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kjv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/Q95565_RAT Q95565_RAT]] Involved in the presentation of foreign antigens to the immune system (By similarity).[SAAS:SAAS003006_004_004364] [[https://www.uniprot.org/uniprot/UBQL1_RAT UBQL1_RAT]] Links CD47 to the cytoskeleton. Promotes the surface expression of GABA-A receptors. Promotes the accumulation of uncleaved PSEN1 and PSEN2 by stimulating their biosynthesis. Has no effect on PSEN1 and PSEN2 degradation (By similarity).<ref>PMID:11528422</ref> [[https://www.uniprot.org/uniprot/B2MG_RAT B2MG_RAT]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
| + | [https://www.uniprot.org/uniprot/Q95565_RAT Q95565_RAT] Involved in the presentation of foreign antigens to the immune system (By similarity).[SAAS:SAAS003006_004_004364] |
| | == 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: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Butcher, G W]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Joly, E]] | + | [[Category: Butcher GW]] |
| - | [[Category: Rudolph, M G]] | + | [[Category: Joly E]] |
| - | [[Category: Speir, J A]] | + | [[Category: Rudolph MG]] |
| - | [[Category: Stevens, J]] | + | [[Category: Speir JA]] |
| - | [[Category: Trowsdale, J]] | + | [[Category: Stevens J]] |
| - | [[Category: Wilson, I A]] | + | [[Category: Trowsdale J]] |
| - | [[Category: Immune system]]
| + | [[Category: Wilson IA]] |
| - | [[Category: Major histocompatibility complex]]
| + | |
| - | [[Category: Peptide-mhc]]
| + | |
| Structural highlights
Function
Q95565_RAT Involved in the presentation of foreign antigens to the immune system (By similarity).[SAAS:SAAS003006_004_004364]
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 PubMed
Antigenic peptides are loaded onto class I MHC molecules in the endoplasmic reticulum (ER) by a complex consisting of the MHC class I heavy chain, beta(2)-microglobulin, calreticulin, tapasin, Erp57 (ER60) and the transporter associated with antigen processing (TAP). While most mammalian species transport these peptides into the ER via a single allele of TAP, rats have evolved different TAPs, TAP-A and TAP-B, that are present in different inbred strains. Each TAP delivers a different spectrum of peptides and is associated genetically with distinct subsets of MHC class Ia alleles, but the molecular basis for the conservation (or co-evolution) of the two transporter alleles is unknown. We have determined the crystal structures of a representative of each MHC subset, viz RT1-A(a) and RT1-A1(c), in association with high-affinity nonamer peptides. The structures reveal how the chemical properties of the two different rat MHC F-pockets match those of the corresponding C termini of the peptides, corroborating biochemical data on the rates of peptide-MHC complex assembly. An unusual sequence in RT1-A1(c) leads to a major deviation from the highly conserved beta(3)/alpha(1) loop (residues 40-59) conformation in mouse and human MHC class I structures. This loop change contributes to profound changes in the shape of the A-pocket in the peptide-binding groove and may explain the function of RT1-A1(c) as an inhibitory natural killer cell ligand.
Crystal structures of two rat MHC class Ia (RT1-A) molecules that are associated differentially with peptide transporter alleles TAP-A and TAP-B.,Rudolph MG, Stevens J, Speir JA, Trowsdale J, Butcher GW, Joly E, Wilson IA J Mol Biol. 2002 Dec 13;324(5):975-90. PMID:12470953[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rudolph MG, Stevens J, Speir JA, Trowsdale J, Butcher GW, Joly E, Wilson IA. Crystal structures of two rat MHC class Ia (RT1-A) molecules that are associated differentially with peptide transporter alleles TAP-A and TAP-B. J Mol Biol. 2002 Dec 13;324(5):975-90. PMID:12470953
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