3qo1
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3qo1 is ON HOLD Authors: Trajtenberg, F., Correa-Bove, A., Buschiazzo, A. Description: Monoclinic form of IgG1 Fab fragment (apo form) sharing same...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Monoclinic form of IgG1 Fab fragment (apo form) sharing same Fv as IgA== | |
| + | <StructureSection load='3qo1' size='340' side='right'caption='[[3qo1]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3qo1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QO1 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=GOL:GLYCEROL'>GOL</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=3qo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qo1 OCA], [https://pdbe.org/3qo1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qo1 RCSB], [https://www.ebi.ac.uk/pdbsum/3qo1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qo1 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Despite being the most abundant class of immunoglobulins in humans and playing central roles in the adaptive immune response, high-resolution structural data are still lacking for the antigen-binding region of human isotype A antibodies (IgAs). The crystal structures of a human Fab fragment of IgA1 in three different crystal forms are now reported. The three-dimensional organization is similar to those of other Fab classes, but FabA1 seems to be more rigid, being constrained by a hydrophobic core in the interface between the variable and constant domains of the heavy chain (VH-CH1) as well as by a disulfide bridge that connects the light and heavy chains, influencing the relative heavy/light-chain orientation. The crystal structure of the same antibody but with a G-isotype CH1 which is reported to display different antigen affinity has also been solved. The differential structural features reveal plausible mechanisms for constant/variable-domain long-distance effects whereby antibody class switching could alter antigen affinity. | ||
| - | + | Structure of a human IgA1 Fab fragment at 1.55 A resolution: potential effect of the constant domains on antigen-affinity modulation.,Correa A, Trajtenberg F, Obal G, Pritsch O, Dighiero G, Oppezzo P, Buschiazzo A Acta Crystallogr D Biol Crystallogr. 2013 Mar;69(Pt 3):388-97. doi:, 10.1107/S0907444912048664. Epub 2013 Feb 16. PMID:23519414<ref>PMID:23519414</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3qo1" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Buschiazzo A]] | ||
| + | [[Category: Correa A]] | ||
| + | [[Category: Trajtenberg F]] | ||
Current revision
Monoclinic form of IgG1 Fab fragment (apo form) sharing same Fv as IgA
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