3qo1

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[[Image:3qo1.png|left|200px]]
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==Monoclinic form of IgG1 Fab fragment (apo form) sharing same Fv as IgA==
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<StructureSection load='3qo1' size='340' side='right' caption='[[3qo1]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3qo1]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QO1 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3m8o|3m8o]], [[3qnx|3qnx]], [[3qny|3qny]], [[3qoz|3qoz]], [[3qo0|3qo0]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qo1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qo1 RCSB], [http://www.ebi.ac.uk/pdbsum/3qo1 PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_3qo1| PDB=3qo1 | SCENE= }}
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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>
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===Monoclinic form of IgG1 Fab fragment (apo form) sharing same Fv as IgA===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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==About this Structure==
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<references/>
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[[3qo1]] is a 2 chain structure with sequence from [http://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].
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Buschiazzo, A.]]
[[Category: Buschiazzo, A.]]

Revision as of 13:15, 18 May 2014

Monoclinic form of IgG1 Fab fragment (apo form) sharing same Fv as IgA

3qo1, resolution 2.40Å

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