1kc5: Difference between revisions
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==CRYSTAL STRUCTURE OF ANTIBODY PC287 IN COMPLEX WITH PS1 PEPTIDE== | ==CRYSTAL STRUCTURE OF ANTIBODY PC287 IN COMPLEX WITH PS1 PEPTIDE== | ||
<StructureSection load='1kc5' size='340' side='right' caption='[[1kc5]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1kc5' size='340' side='right' caption='[[1kc5]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
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<table><tr><td colspan='2'>[[1kc5]] is a 3 chain structure with sequence 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=1KC5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KC5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1kc5]] is a 3 chain structure with sequence 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=1KC5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KC5 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kcr|1kcr]], [[1kcs|1kcs]], [[1kcu|1kcu]], [[1kcv|1kcv]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kcr|1kcr]], [[1kcs|1kcs]], [[1kcu|1kcu]], [[1kcv|1kcv]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kc5 OCA], [http://pdbe.org/1kc5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kc5 RCSB], [http://www.ebi.ac.uk/pdbsum/1kc5 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kc5 OCA], [http://pdbe.org/1kc5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kc5 RCSB], [http://www.ebi.ac.uk/pdbsum/1kc5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kc5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kc/1kc5_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kc/1kc5_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 00:40, 25 January 2018
CRYSTAL STRUCTURE OF ANTIBODY PC287 IN COMPLEX WITH PS1 PEPTIDECRYSTAL STRUCTURE OF ANTIBODY PC287 IN COMPLEX WITH PS1 PEPTIDE
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCrystal structures of distinct mAbs that recognize a common epitope of a peptide Ag have been determined and analyzed in the unbound and bound forms. These Abs display dissimilar binding site structures in the absence of the Ag. The dissimilarity is primarily expressed in the conformations of complementarity-determining region H3, which is responsible for defining the epitope specificity. Interestingly, however, the three Abs exhibit similar complementarity-determining region conformations in the Ag binding site while recognizing the common epitope, indicating that different pathways of binding are used for Ag recognition. The epitope also exhibits conformational similarity when bound to each of these Abs, although the peptide Ag was otherwise flexible. The observed conformational convergence in the epitope and the Ag binding site was facilitated by the plasticity in the nature of interactions. Epitope recognition by diverse antibodies suggests conformational convergence in an antibody response.,Nair DT, Singh K, Siddiqui Z, Nayak BP, Rao KV, Salunke DM J Immunol. 2002 Mar 1;168(5):2371-82. PMID:11859128[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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