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[[Image:1jpf.jpg|left|200px]]
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{{STRUCTURE_1jpf|  PDB=1jpf  |  SCENE=  }}
'''Crystal Structure Of The LCMV Peptidic Epitope Gp276 In Complex With The Murine Class I Mhc Molecule H-2Db'''


==Crystal Structure Of The LCMV Peptidic Epitope Gp276 In Complex With The Murine Class I Mhc Molecule H-2Db==
<StructureSection load='1jpf' size='340' side='right'caption='[[1jpf]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jpf]] 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=1JPF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JPF 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=1jpf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jpf OCA], [https://pdbe.org/1jpf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jpf RCSB], [https://www.ebi.ac.uk/pdbsum/1jpf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jpf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HA11_MOUSE HA11_MOUSE] Involved in the presentation of foreign antigens to the immune system.
== 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/jp/1jpf_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=1jpf ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Class I major histocompatibility complex (MHC) molecules, which display intracellularly processed peptides on the cell surface for scanning by T-cell receptors (TCRs), are extraordinarily polymorphic. MHC polymorphism is believed to result from natural selection, since individuals heterozygous at the corresponding loci can cope with a larger number of pathogens. Here, we present the crystal structures of the murine MHC molecule H-2D(b) in complex with the peptides gp276 and np396 from the lymphocytic choriomeningitis virus (LCMV), solved at 2.18 A and 2.20 A resolution, respectively. The most prominent feature of H-2D(b) is a hydrophobic ridge that cuts across its antigen-binding site, which is conserved in the L(d)-like family of class I MHC molecules. The comparison with previously solved crystal structures of peptide/H-2D(b) complexes shows that the hydrophobic ridge focuses the conformational variability of the bound peptides in a "hot-spot", which could allow optimal TCR interaction and discrimination. This finding suggests a functional reason for the conservation of this structural element.


==Overview==
Zooming in on the hydrophobic ridge of H-2D(b): implications for the conformational variability of bound peptides.,Ciatto C, Tissot AC, Tschopp M, Capitani G, Pecorari F, Pluckthun A, Grutter MG J Mol Biol. 2001 Oct 5;312(5):1059-71. PMID:11580250<ref>PMID:11580250</ref>
Class I major histocompatibility complex (MHC) molecules, which display intracellularly processed peptides on the cell surface for scanning by T-cell receptors (TCRs), are extraordinarily polymorphic. MHC polymorphism is believed to result from natural selection, since individuals heterozygous at the corresponding loci can cope with a larger number of pathogens. Here, we present the crystal structures of the murine MHC molecule H-2D(b) in complex with the peptides gp276 and np396 from the lymphocytic choriomeningitis virus (LCMV), solved at 2.18 A and 2.20 A resolution, respectively. The most prominent feature of H-2D(b) is a hydrophobic ridge that cuts across its antigen-binding site, which is conserved in the L(d)-like family of class I MHC molecules. The comparison with previously solved crystal structures of peptide/H-2D(b) complexes shows that the hydrophobic ridge focuses the conformational variability of the bound peptides in a "hot-spot", which could allow optimal TCR interaction and discrimination. This finding suggests a functional reason for the conservation of this structural element.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1JPF is a [[Protein complex]] structure of sequences 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=1JPF OCA].
</div>
<div class="pdbe-citations 1jpf" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Zooming in on the hydrophobic ridge of H-2D(b): implications for the conformational variability of bound peptides., Ciatto C, Tissot AC, Tschopp M, Capitani G, Pecorari F, Pluckthun A, Grutter MG, J Mol Biol. 2001 Oct 5;312(5):1059-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11580250 11580250]
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
*[[MHC 3D structures|MHC 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Capitani G]]
[[Category: Capitani, G.]]
[[Category: Ciatto C]]
[[Category: Ciatto, C.]]
[[Category: Grutter MG]]
[[Category: Grutter, M G.]]
[[Category: Pecorari F]]
[[Category: Pecorari, F.]]
[[Category: Pluckthun A]]
[[Category: Pluckthun, A.]]
[[Category: Tissot AC]]
[[Category: Tissot, A C.]]
[[Category: Tschopp M]]
[[Category: Tschopp, M.]]
[[Category: Ig fold]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:33:04 2008''