2h2r: Difference between revisions
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'''Crystal structure of the human CD23 Lectin domain, apo form''' | '''Crystal structure of the human CD23 Lectin domain, apo form''' | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Wurzburg, B A.]] | [[Category: Wurzburg, B A.]] | ||
[[Category: | [[Category: Apo form]] | ||
[[Category: | [[Category: C-type lectin]] | ||
[[Category: | [[Category: Lectin domain]] | ||
[[Category: | [[Category: Low affinity ige receptor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:48:06 2008'' | |||
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Revision as of 05:48, 4 May 2008
Crystal structure of the human CD23 Lectin domain, apo form
OverviewOverview
CD23, the low-affinity receptor for IgE (Fc epsilonRII), regulates IgE synthesis and also mediates IgE-dependent antigen transport and processing. CD23 is a unique Fc receptor belonging to the C-type lectin-like domain superfamily and binds IgE in an unusual, non-lectin-like manner, requiring calcium but not carbohydrate. We have solved the high-resolution crystal structures of the human CD23 lectin domain in the presence and absence of Ca2+. The crystal structures differ significantly from a previously determined NMR structure and show that calcium binding occurs at the principal binding site, but not at an auxiliary site that appears to be absent in human CD23. Conformational differences between the apo and Ca2+ bound structures suggest how IgE-Fc binding can be both calcium-dependent and carbohydrate-independent.
About this StructureAbout this Structure
2H2R is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural changes in the lectin domain of CD23, the low-affinity IgE receptor, upon calcium binding., Wurzburg BA, Tarchevskaya SS, Jardetzky TS, Structure. 2006 Jun;14(6):1049-58. PMID:16765898 Page seeded by OCA on Sun May 4 05:48:06 2008