1dl7: Difference between revisions

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New page: left|200px<br /> <applet load="1dl7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dl7, resolution 2.35Å" /> '''THE STRUCTURAL BASI...
 
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[[Image:1dl7.gif|left|200px]]<br />
<applet load="1dl7" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1dl7, resolution 2.35&Aring;" />
'''THE STRUCTURAL BASIS OF REPERTOIRE SHIFT IN AN IMMUNE RESPONSE TO PHOSPHOCHOLINE'''<br />


==Overview==
==THE STRUCTURAL BASIS OF REPERTOIRE SHIFT IN AN IMMUNE RESPONSE TO PHOSPHOCHOLINE==
The immune response to phosphocholine (PC)-protein is characterized by a, shift in antibody repertoire as the response progresses. This change in, expressed gene combinations is accompanied by a shift in fine specificity, toward the carrier, resulting in high affinity to PC-protein. The, somatically mutated memory hybridoma, M3C65, possesses high affinity for, PC-protein and the phenyl-hapten analogue, p-nitrophenyl phosphocholine, (NPPC). Affinity measurements using related PC-phenyl analogues, including, peptides of varying lengths, demonstrate that carrier determinants, contribute to binding affinity and that somatic mutations alter this, recognition. The crystal structure of an M3C65-NPPC complex at 2.35-A, resolution allows evaluation of the three light chain mutations that, confer high-affinity binding to NPPC. Only one of the mutations involves a, contact residue, whereas the other two have indirect effects on the shape, of the combining site. Comparison of the M3C65 structure to that of T15, an antibody dominating the primary response, provides clear structural, evidence for the role of carrier determinants in promoting repertoire, shift. These two antibodies express unrelated variable region heavy and, light chain genes and represent a classic example of the effect of, repertoire shift on maturation of the immune response.
<StructureSection load='1dl7' size='340' side='right'caption='[[1dl7]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1dl7]] is a 2 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=1DL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DL7 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]] 2.35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NCH:P-NITROPHENYL-PHOSPHOCHOLINE'>NCH</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=1dl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dl7 OCA], [https://pdbe.org/1dl7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dl7 RCSB], [https://www.ebi.ac.uk/pdbsum/1dl7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dl7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LV1B_MOUSE LV1B_MOUSE]
== 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/dl/1dl7_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=1dl7 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1DL7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NCH as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DL7 OCA].
*[[Antibody 3D structures|Antibody 3D structures]]
 
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
==Reference==
__TOC__
The structural basis of repertoire shift in an immune response to phosphocholine., Brown M, Schumacher MA, Wiens GD, Brennan RG, Rittenberg MB, J Exp Med. 2000 Jun 19;191(12):2101-12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10859335 10859335]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Mus musculus]]
[[Category: Brown, M.]]
[[Category: Brown M]]
[[Category: Schumacher, M.]]
[[Category: Schumacher M]]
[[Category: NCH]]
[[Category: repertoire shift]]
[[Category: single chain fv]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:28:29 2007''

Latest revision as of 12:51, 20 March 2024

THE STRUCTURAL BASIS OF REPERTOIRE SHIFT IN AN IMMUNE RESPONSE TO PHOSPHOCHOLINETHE STRUCTURAL BASIS OF REPERTOIRE SHIFT IN AN IMMUNE RESPONSE TO PHOSPHOCHOLINE

Structural highlights

1dl7 is a 2 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 2.35Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LV1B_MOUSE

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1dl7, resolution 2.35Å

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OCA
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