3qny

Monoclinic form of human IgA1 Fab fragment, sharing same Fv as IgG

spinqualitylabelsall models 3qny, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qny is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL Related: 3m8o, 3qnx, 3qnz, 3qo0, 3qo1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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