1kcs
From Proteopedia
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| - | [[Image:1kcs.jpg|left|200px]] | ||
| - | + | ==CRYSTAL STRUCTURE OF ANTIBODY PC282 IN COMPLEX WITH PS1 PEPTIDE== | |
| - | + | <StructureSection load='1kcs' size='340' side='right'caption='[[1kcs]], [[Resolution|resolution]] 2.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1kcs]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Hepatitis_B_virus_genotype_A1_subtype_adw2_(Isolate_South_Africa/84/2001) Hepatitis B virus genotype A1 subtype adw2 (Isolate South Africa/84/2001)] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KCS 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]] 2.5Å</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=1kcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kcs OCA], [https://pdbe.org/1kcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kcs RCSB], [https://www.ebi.ac.uk/pdbsum/1kcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kcs ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | ''' | + | [https://www.uniprot.org/uniprot/IGKC_MOUSE IGKC_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/kc/1kcs_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1kcs ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Crystal 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. | Crystal 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<ref>PMID:11859128</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1kcs" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | + | [[Category: Nair DT]] | |
| - | [[Category: Nair | + | [[Category: Nayak BP]] |
| - | [[Category: Nayak | + | [[Category: Rao KVS]] |
| - | [[Category: Rao | + | [[Category: Salunke DM]] |
| - | [[Category: Salunke | + | [[Category: Siddiqui Z]] |
| - | [[Category: Siddiqui | + | [[Category: Singh K]] |
| - | [[Category: Singh | + | |
| - | + | ||
| - | + | ||
Current revision
CRYSTAL STRUCTURE OF ANTIBODY PC282 IN COMPLEX WITH PS1 PEPTIDE
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Categories: Large Structures | Mus musculus | Nair DT | Nayak BP | Rao KVS | Salunke DM | Siddiqui Z | Singh K
