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[[Image:1nan.gif|left|200px]]
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{{STRUCTURE_1nan|  PDB=1nan  |  SCENE=  }}
'''MCH CLASS I H-2KB MOLECULE COMPLEXED WITH PBM1 PEPTIDE'''


==MCH CLASS I H-2KB MOLECULE COMPLEXED WITH PBM1 PEPTIDE==
<StructureSection load='1nan' size='340' side='right'caption='[[1nan]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1nan]] is a 6 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=1NAN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NAN 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]] 2.3&#8491;</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=1nan FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nan OCA], [https://pdbe.org/1nan PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nan RCSB], [https://www.ebi.ac.uk/pdbsum/1nan PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nan ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B2MG_MOUSE B2MG_MOUSE] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide 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/na/1nan_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1nan ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
T cell receptor (TCR) binding degeneracy lies at the heart of several physiological and pathological phenomena, yet its structural basis is poorly understood. We determined the crystal structure of a complex involving the BM3.3 TCR and an octapeptide (VSV8) bound to the H-2K(b) major histocompatibility complex molecule at a 2.7 A resolution, and compared it with the BM3.3 TCR bound to the H-2K(b) molecule loaded with a peptide that has no primary sequence identity with VSV8. Comparison of these structures showed that the BM3.3 TCR complementarity-determining region (CDR) 3alpha could undergo rearrangements to adapt to structurally different peptide residues. Therefore, CDR3 loop flexibility helps explain TCR binding cross-reactivity.


==Overview==
CDR3 loop flexibility contributes to the degeneracy of TCR recognition.,Reiser JB, Darnault C, Gregoire C, Mosser T, Mazza G, Kearney A, van der Merwe PA, Fontecilla-Camps JC, Housset D, Malissen B Nat Immunol. 2003 Mar;4(3):241-7. Epub 2003 Feb 3. PMID:12563259<ref>PMID:12563259</ref>
T cell receptor (TCR) binding degeneracy lies at the heart of several physiological and pathological phenomena, yet its structural basis is poorly understood. We determined the crystal structure of a complex involving the BM3.3 TCR and an octapeptide (VSV8) bound to the H-2K(b) major histocompatibility complex molecule at a 2.7 A resolution, and compared it with the BM3.3 TCR bound to the H-2K(b) molecule loaded with a peptide that has no primary sequence identity with VSV8. Comparison of these structures showed that the BM3.3 TCR complementarity-determining region (CDR) 3alpha could undergo rearrangements to adapt to structurally different peptide residues. Therefore, CDR3 loop flexibility helps explain TCR binding cross-reactivity.


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


==Reference==
==See Also==
CDR3 loop flexibility contributes to the degeneracy of TCR recognition., Reiser JB, Darnault C, Gregoire C, Mosser T, Mazza G, Kearney A, van der Merwe PA, Fontecilla-Camps JC, Housset D, Malissen B, Nat Immunol. 2003 Mar;4(3):241-7. Epub 2003 Feb 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12563259 12563259]
*[[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: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Darnault C]]
[[Category: Darnault, C.]]
[[Category: Fontecilla-Camps JC]]
[[Category: Fontecilla-Camps, J C.]]
[[Category: Gregoire C]]
[[Category: Gregoire, C.]]
[[Category: Housset D]]
[[Category: Housset, D.]]
[[Category: Kearnay A]]
[[Category: Kearnay, A.]]
[[Category: Malissen B]]
[[Category: Malissen, B.]]
[[Category: Mazza G]]
[[Category: Mazza, G.]]
[[Category: Mosser T]]
[[Category: Merwe, P A.van der.]]
[[Category: Reiser J-B]]
[[Category: Mosser, T.]]
[[Category: Van der Merwe PA]]
[[Category: Reiser, J B.]]
[[Category: Alloreactivity]]
[[Category: Class i mhc]]
[[Category: Crossreactivity]]
[[Category: H-2kb]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:18:01 2008''
Retrieved from "https://proteopedia.org/1nan"