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New page: left|200px<br /><applet load="1kjv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kjv, resolution 1.48Å" /> '''TAP-B-associated rat...
 
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[[Image:1kjv.jpg|left|200px]]<br /><applet load="1kjv" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1kjv, resolution 1.48&Aring;" />
'''TAP-B-associated rat MHC class I molecule'''<br />


==Overview==
==TAP-B-associated rat MHC class I molecule==
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.
<StructureSection load='1kjv' size='340' side='right'caption='[[1kjv]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.48&#8491;</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>
</table>
== 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]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kj/1kjv_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kjv ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==About this Structure==
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<ref>PMID:12470953</ref>
1KJV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KJV OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12470953 12470953]
</div>
[[Category: Protein complex]]
<div class="pdbe-citations 1kjv" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
*[[MHC 3D structures|MHC 3D structures]]
*[[MHC I 3D structures|MHC I 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Butcher, G.W.]]
[[Category: Butcher GW]]
[[Category: Joly, E.]]
[[Category: Joly E]]
[[Category: Rudolph, M.G.]]
[[Category: Rudolph MG]]
[[Category: Speir, J.A.]]
[[Category: Speir JA]]
[[Category: Stevens, J.]]
[[Category: Stevens J]]
[[Category: Trowsdale, J.]]
[[Category: Trowsdale J]]
[[Category: Wilson, I.A.]]
[[Category: Wilson IA]]
[[Category: SO4]]
[[Category: major histocompatibility complex]]
[[Category: peptide-mhc]]
 
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