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| | <StructureSection load='3o11' size='340' side='right'caption='[[3o11]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='3o11' size='340' side='right'caption='[[3o11]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3o11]] is a 4 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=3O11 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O11 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3o11]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=3O11 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O11 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mcl|3mcl]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IGKC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), IGHG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3o11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o11 OCA], [https://pdbe.org/3o11 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o11 RCSB], [https://www.ebi.ac.uk/pdbsum/3o11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o11 ProSAT]</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=3o11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o11 OCA], [http://pdbe.org/3o11 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o11 RCSB], [http://www.ebi.ac.uk/pdbsum/3o11 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o11 ProSAT]</span></td></tr> | + | |
| | </table> | | </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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o1/3o11_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o1/3o11_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Gilliland, G L]] | + | [[Category: Gilliland GL]] |
| - | [[Category: Malia, T]] | + | [[Category: Malia T]] |
| - | [[Category: Obmolova, G]] | + | [[Category: Obmolova G]] |
| - | [[Category: Teplyakov, A]] | + | [[Category: Teplyakov A]] |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Immunoglobulin fold]]
| + | |
| Structural highlights
Disease
IGKC_HUMAN Defects in IGKC are the cause of immunoglobulin kappa light chain deficiency (IGKCD) [MIM:614102. IGKCD is a disease characterized by the complete absence of immunoglobulin kappa chains.[1]
Function
IGKC_HUMAN
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 PubMed
Alzheimer's disease is a progressive neurodegenerative disease characterized by extracellular deposits of beta-amyloid (Abeta) plaques. Aggregation of the Abeta(42) peptide leading to plaque formation is believed to play a central role in Alzheimer's disease pathogenesis. Anti-Abeta monoclonal antibodies can reduce amyloid plaques and could possibly be used for immunotherapy. We have developed a monoclonal antibody C706, which recognizes the human Abeta peptide. Here we report the crystal structure of the antibody Fab fragment at 1.7 A resolution. The structure was determined in two crystal forms, P2(1) and C2. Although the Fab was crystallized in the presence of Abeta(16), no peptide was observed in the crystals. The antigen-binding site is blocked by the hexahistidine tag of another Fab molecule in both crystal forms. The poly-His peptide in an extended conformation occupies a crevice between the light and heavy chains of the variable domain. Two consecutive histidines (His4-His5) stack against tryptophan residues in the central pocket of the antigen-binding surface. In addition, they form hydrogen bonds to the acidic residues at the bottom of the pocket. The mode of his-tag binding by C706 resembles the Abeta recognition by antibodies PFA1 and WO2. All three antibodies recognize the same immunodominant B-cell epitope of Abeta. By similarity, residues Phe-Arg-His of Abeta would be a major portion of the C706 epitope. Copyright (c) 2010 John Wiley & Sons, Ltd.
His-tag binding by antibody C706 mimics beta-amyloid recognition.,Teplyakov A, Obmolova G, Canziani G, Zhao Y, Gutshall L, Jung SS, Gilliland GL J Mol Recognit. 2010 Sep 14. PMID:20842634[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stavnezer-Nordgren J, Kekish O, Zegers BJ. Molecular defects in a human immunoglobulin kappa chain deficiency. Science. 1985 Oct 25;230(4724):458-61. PMID:3931219
- ↑ Teplyakov A, Obmolova G, Canziani G, Zhao Y, Gutshall L, Jung SS, Gilliland GL. His-tag binding by antibody C706 mimics beta-amyloid recognition. J Mol Recognit. 2010 Sep 14. PMID:20842634 doi:10.1002/jmr.1069
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