1a4k
From Proteopedia
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| - | {{STRUCTURE_1a4k| PDB=1a4k | SCENE= }} | ||
| - | ===DIELS ALDER CATALYTIC ANTIBODY WITH TRANSITION STATE ANALOGUE=== | ||
| - | {{ABSTRACT_PUBMED_9506942}} | ||
| - | == | + | ==DIELS ALDER CATALYTIC ANTIBODY WITH TRANSITION STATE ANALOGUE== |
| - | [[http://www.uniprot.org/uniprot/IGKC_HUMAN IGKC_HUMAN | + | <StructureSection load='1a4k' size='340' side='right'caption='[[1a4k]], [[Resolution|resolution]] 2.40Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1a4k]] 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=1A4K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A4K 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]] 2.4Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=FRA:[4-(4-ACETYLAMINO-PHENYL)-3,5-DIOXO-4-AZA-TRICYCLO[5.2.2.0+2,6]UNDEC-1-YLCARBAMOYLOXY]-ACETIC+ACID'>FRA</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=1a4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4k OCA], [https://pdbe.org/1a4k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a4k RCSB], [https://www.ebi.ac.uk/pdbsum/1a4k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a4k ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/IGKC_HUMAN IGKC_HUMAN] Defects in IGKC are the cause of immunoglobulin kappa light chain deficiency (IGKCD) [MIM:[https://omim.org/entry/614102 614102]. IGKCD is a disease characterized by the complete absence of immunoglobulin kappa chains.<ref>PMID:3931219</ref> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/IGKC_HUMAN IGKC_HUMAN] | ||
| + | == 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/a4/1a4k_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=1a4k ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The three-dimensional structure of an antibody (39-A11) that catalyzes a Diels-Alder reaction has been determined. The structure suggests that the antibody catalyzes this pericyclic reaction through a combination of packing and hydrogen-bonding interactions that control the relative geometries of the bound substrates and electronic distribution in the dienophile. A single somatic mutation, serine-91 of the light chain to valine, is largely responsible for the increase in affinity and catalytic activity of the affinity-matured antibody. Structural and functional studies of the germ-line precursor suggest that 39-A11 and related antibodies derive from a family of germ-line genes that have been selected throughout evolution for the ability of the encoded proteins to form a polyspecific combining site. Germ line-encoded antibodies of this type, which can rapidly evolve into high-affinity receptors for a broad range of structures, may help to expand the binding potential associated with the structural diversity of the primary antibody repertoire. | ||
| - | + | Immunological origins of binding and catalysis in a Diels-Alderase antibody.,Romesberg FE, Spiller B, Schultz PG, Stevens RC Science. 1998 Mar 20;279(5358):1929-33. PMID:9506942<ref>PMID:9506942</ref> | |
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| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | <div class="pdbe-citations 1a4k" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Romesburg | + | [[Category: Romesburg FE]] |
| - | [[Category: Schultz | + | [[Category: Schultz PG]] |
| - | [[Category: Spiller | + | [[Category: Spiller BW]] |
| - | [[Category: Stevens | + | [[Category: Stevens RC]] |
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Current revision
DIELS ALDER CATALYTIC ANTIBODY WITH TRANSITION STATE ANALOGUE
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