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4j6n

From Proteopedia

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m (Protected "4j6n" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4j6n| PDB=4j6n | SCENE= }}
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===Crystal structure of calcium2+-free wild-type CD23 lectin domain (crystal form E)===
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{{ABSTRACT_PUBMED_23933509}}
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The entry 4j6n is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/FCER2_HUMAN FCER2_HUMAN]] Low-affinity receptor for immunoglobulin E (IgE) and CR2/CD21. Has essential roles in the regulation of IgE production and in the differentiation of B-cells (it is a B-cell-specific antigen).
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Authors: Dhaliwal, B., Pang, M.O.Y., Sutton, B.J.
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==About this Structure==
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[[4j6n]] 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=4J6N OCA].
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Description: Crystal structure of calcium2+-free wild-type CD23 lectin domain (crystal form E)
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==Reference==
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<ref group="xtra">PMID:023933509</ref><references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Dhaliwal, B.]]
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[[Category: Pang, M O.Y.]]
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[[Category: Sutton, B J.]]
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[[Category: Antibody receptor]]
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[[Category: Immune system]]
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[[Category: Immunoglobulin fold lectin]]

Revision as of 07:32, 28 August 2013

Template:STRUCTURE 4j6n

Contents

Crystal structure of calcium2+-free wild-type CD23 lectin domain (crystal form E)

Template:ABSTRACT PUBMED 23933509

Function

[FCER2_HUMAN] Low-affinity receptor for immunoglobulin E (IgE) and CR2/CD21. Has essential roles in the regulation of IgE production and in the differentiation of B-cells (it is a B-cell-specific antigen).

About this Structure

4j6n is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Dhaliwal B, Pang MO, Yuan D, Yahya N, Fabiane SM, McDonnell JM, Gould HJ, Beavil AJ, Sutton BJ. Conformational plasticity at the IgE-binding site of the B-cell receptor CD23. Mol Immunol. 2013 Aug 6;56(4):693-697. doi: 10.1016/j.molimm.2013.07.005. PMID:23933509 doi:10.1016/j.molimm.2013.07.005

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OCA

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