1cic: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1cic]] is a 4 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=1CIC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CIC FirstGlance]. <br> | <table><tr><td colspan='2'>[[1cic]] is a 4 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=1CIC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CIC 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=1cic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cic OCA], [https://pdbe.org/1cic PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cic RCSB], [https://www.ebi.ac.uk/pdbsum/1cic PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cic ProSAT]</span></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]] 2.5Å</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=1cic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cic OCA], [https://pdbe.org/1cic PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cic RCSB], [https://www.ebi.ac.uk/pdbsum/1cic PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cic ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/IGKC_MOUSE IGKC_MOUSE] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Bentley | [[Category: Bentley GA]] | ||
Revision as of 02:26, 28 December 2023
IDIOTOPE-ANTI-IDIOTOPE FAB-FAB COMPLEX; D1.3-E225IDIOTOPE-ANTI-IDIOTOPE FAB-FAB COMPLEX; D1.3-E225
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSerologically detected antigenic determinants unique to an antibody or group of antibodies are called idiotopes. The sum of idiotopes of an antibody constitute its idiotype. Idiotypes have been intensively studied following a hypothesis for the self-regulation of the immune system through a network of idiotype-anti-idiotype interactions. Furthermore, as antigen and anti-idiotypes can competitively bind to idiotype-positive, antigen-specific antibodies, anti-idiotypes may carry an 'internal image' of the external antigen. Here we describe the structure of the complex between the monoclonal anti-lysozyme FabD1.3 and the anti-idiotopic FabE225 at 2.5 A resolution. This complex defines a private idiotope consisting of 13 amino-acid residues, mainly from the complementarity-determining regions of D1.3. Seven of these residues make contacts with the antigen, indicating a significant overlap between idiotope and antigen-combining site. Idiotopic mimicry of the external antigen is not achieved at the molecular level in this example. Three-dimensional structure of an idiotope-anti-idiotope complex.,Bentley GA, Boulot G, Riottot MM, Poljak RJ Nature. 1990 Nov 15;348(6298):254-7. PMID:1700305[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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