4ki1: Difference between revisions
No edit summary |
No edit summary |
||
| Line 8: | Line 8: | ||
<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=4ki1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ki1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ki1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ki1 PDBsum]</span></td></tr> | <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=4ki1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ki1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ki1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ki1 PDBsum]</span></td></tr> | ||
<table> | <table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The antibody IgE plays a central role in allergic disease, functioning principally through two cell-surface receptors: FcRI and CD23. FcRI on mast cells and basophils mediates the immediate hypersensitivity response, whilst the interaction of IgE with CD23 on B cells regulates IgE production. Crystal structures of the lectin-like `head' domain of CD23 alone and bound to a subfragment of IgE consisting of the dimer of C3 and C4 domains (Fc3-4) have recently been determined, revealing flexibility in the IgE-binding site of CD23. Here, a new crystal form of the CD23-Fc3-4 complex with different molecular-packing constraints is reported, which together with the earlier results demonstrates that conformational variability at the interface extends additionally to the IgE Fc and the quaternary structure of its domains. | |||
A range of C3-C4 interdomain angles in IgE Fc accommodate binding to its receptor CD23.,Dhaliwal B, Pang MO, Yuan D, Beavil AJ, Sutton BJ Acta Crystallogr F Struct Biol Commun. 2014 Mar;70(Pt 3):305-9. doi:, 10.1107/S2053230X14003355. Epub 2014 Feb 20. PMID:24598915<ref>PMID:24598915</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:52, 24 September 2014
Primitive triclinic crystal form of the human IgE-Fc(epsilon)3-4 bound to its B cell receptor derCD23Primitive triclinic crystal form of the human IgE-Fc(epsilon)3-4 bound to its B cell receptor derCD23
Structural highlights
Publication Abstract from PubMedThe antibody IgE plays a central role in allergic disease, functioning principally through two cell-surface receptors: FcRI and CD23. FcRI on mast cells and basophils mediates the immediate hypersensitivity response, whilst the interaction of IgE with CD23 on B cells regulates IgE production. Crystal structures of the lectin-like `head' domain of CD23 alone and bound to a subfragment of IgE consisting of the dimer of C3 and C4 domains (Fc3-4) have recently been determined, revealing flexibility in the IgE-binding site of CD23. Here, a new crystal form of the CD23-Fc3-4 complex with different molecular-packing constraints is reported, which together with the earlier results demonstrates that conformational variability at the interface extends additionally to the IgE Fc and the quaternary structure of its domains. A range of C3-C4 interdomain angles in IgE Fc accommodate binding to its receptor CD23.,Dhaliwal B, Pang MO, Yuan D, Beavil AJ, Sutton BJ Acta Crystallogr F Struct Biol Commun. 2014 Mar;70(Pt 3):305-9. doi:, 10.1107/S2053230X14003355. Epub 2014 Feb 20. PMID:24598915[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||