1lk2: Difference between revisions

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New page: left|200px<br /><applet load="1lk2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lk2, resolution 1.35Å" /> '''1.35A crystal struct...
 
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[[Image:1lk2.gif|left|200px]]<br /><applet load="1lk2" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1lk2, resolution 1.35&Aring;" />
'''1.35A crystal structure of H-2Kb complexed with the GNYSFYAL peptide'''<br />


==Overview==
==1.35A crystal structure of H-2Kb complexed with the GNYSFYAL peptide==
We identify and consider some characteristics of a peptide antagonist for, the Ag-specific receptor on 2C cells (the 2C TCR). The peptide, GNYSFYAL, (called GNY), binds to H-2K(b), and a very high-resolution crystal, structure of the GNY-K(b) complex at 1.35 A is described. Although the GNY, peptide does not bind to L(d), the potency of GNY-K(b) as an antagonist is, evident from its ability to specifically inhibit 2C TCR-mediated reactions, to an allogenic agonist complex (QLSPFPFDL-L(d)), as well as to a, syngeneic agonist complex (SIYRYYGL-K(b)). The crystal structure and the, activities of alanine-substituted peptide variants point to the properties, of the peptide P4 side chain and the conformation of the Tyr-P6 side chain, as the structural determinants of GNYSFYAL antagonist activity.
<StructureSection load='1lk2' size='340' side='right'caption='[[1lk2]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lk2]] 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=1LK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LK2 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]] 1.35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1lk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lk2 OCA], [https://pdbe.org/1lk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lk2 RCSB], [https://www.ebi.ac.uk/pdbsum/1lk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lk2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HA1B_MOUSE HA1B_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/lk/1lk2_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=1lk2 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1LK2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG, PO4, MRD and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LK2 OCA].
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
 
*[[MHC 3D structures|MHC 3D structures]]
==Reference==
*[[MHC I 3D structures|MHC I 3D structures]]
A peptide that antagonizes TCR-mediated reactions with both syngeneic and allogeneic agonists: functional and structural aspects., Rudolph MG, Shen LQ, Lamontagne SA, Luz JG, Delaney JR, Ge Q, Cho BK, Palliser D, McKinley CA, Chen J, Wilson IA, Eisen HN, J Immunol. 2004 Mar 1;172(5):2994-3002. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14978103 14978103]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Eisen H]]
[[Category: Eisen, H.]]
[[Category: Luz JG]]
[[Category: Luz, J.G.]]
[[Category: Rudolph MG]]
[[Category: Rudolph, M.G.]]
[[Category: Wilson IA]]
[[Category: Wilson, I.A.]]
[[Category: MPD]]
[[Category: MRD]]
[[Category: NAG]]
[[Category: PO4]]
[[Category: anisotropic and tls refinement]]
[[Category: class i mhc-peptide complex]]
[[Category: high resolution]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:36:58 2007''

Latest revision as of 11:10, 3 April 2024

1.35A crystal structure of H-2Kb complexed with the GNYSFYAL peptide1.35A crystal structure of H-2Kb complexed with the GNYSFYAL peptide

Structural highlights

1lk2 is a 3 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.35Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HA1B_MOUSE 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.

See Also

1lk2, resolution 1.35Å

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