3qnx
From Proteopedia
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| - | [[Image:3qnx.png|left|200px]] | ||
| - | + | ==Orthorhombic form of human IgA1 Fab fragment, sharing same Fv as IgG== | |
| + | <StructureSection load='3qnx' size='340' side='right'caption='[[3qnx]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3qnx]] 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=3QNX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QNX 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]] 2.2Å</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=3qnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qnx OCA], [https://pdbe.org/3qnx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qnx RCSB], [https://www.ebi.ac.uk/pdbsum/3qnx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qnx 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 3qnx" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Buschiazzo A]] |
| - | [[Category: | + | [[Category: Correa A]] |
| - | [[Category: | + | [[Category: Trajtenberg F]] |
| - | + | ||
Current revision
Orthorhombic form of human IgA1 Fab fragment, sharing same Fv as IgG
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