2h2t

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(New page: 200px<br /> <applet load="2h2t" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h2t, resolution 1.30&Aring;" /> '''CD23 Lectin domain,...)
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[[Image:2h2t.gif|left|200px]]<br />
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[[Image:2h2t.gif|left|200px]]<br /><applet load="2h2t" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2h2t" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2h2t, resolution 1.30&Aring;" />
caption="2h2t, resolution 1.30&Aring;" />
'''CD23 Lectin domain, Calcium 2+-bound'''<br />
'''CD23 Lectin domain, Calcium 2+-bound'''<br />
==Overview==
==Overview==
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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.
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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 Structure==
==About this Structure==
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2H2T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2H2T OCA].
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2H2T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H2T OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Wurzburg, B.A.]]
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[[Category: Wurzburg, B A.]]
[[Category: CA]]
[[Category: CA]]
[[Category: c-type lectin]]
[[Category: c-type lectin]]
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[[Category: low affinity ige receptor]]
[[Category: low affinity ige receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:25:28 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:37:39 2008''

Revision as of 15:37, 21 February 2008


2h2t, resolution 1.30Å

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CD23 Lectin domain, Calcium 2+-bound

Overview

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 Structure

2H2T is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

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

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