1dl7: Difference between revisions

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 <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 [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1DL7 FirstGlance]. <br>
+<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='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>
+</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HYBRIDOMA M3C65 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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'>[http://proteopedia.org/fgij/fg.htm?mol=1dl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dl7 OCA], [http://pdbe.org/1dl7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dl7 RCSB], [http://www.ebi.ac.uk/pdbsum/1dl7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dl7 ProSAT]</span></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]]
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 </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>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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:10859335<ref>PMID:10859335</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1dl7" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Antibody 3D structures|Antibody 3D structures]]
 *[[3D structures of non-human antibody|3D structures of non-human antibody]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Brown, M]]
+[[Category: Brown M]]
-[[Category: Schumacher, M]]
+[[Category: Schumacher M]]
-[[Category: Immune system]]
-[[Category: Repertoire shift]]
-[[Category: Single chain fv]]