4j6m: Difference between revisions

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{{STRUCTURE_4j6m|  PDB=4j6m  |  SCENE=  }}
===Crystal structure of calcium2+-free wild-type CD23 lectin domain (crystal form D)===
{{ABSTRACT_PUBMED_23933509}}


==Function==
==Crystal structure of calcium2+-free wild-type CD23 lectin domain (crystal form D)==
[[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).  
<StructureSection load='4j6m' size='340' side='right'caption='[[4j6m]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4j6m]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J6M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J6M FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.48&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4j6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j6m OCA], [https://pdbe.org/4j6m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j6m RCSB], [https://www.ebi.ac.uk/pdbsum/4j6m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j6m ProSAT]</span></td></tr>
</table>
== Function ==
[https://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).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
IgE antibodies play a central role in allergic disease. They recognize allergens via their Fab regions, whilst their effector functions are controlled through interactions of the Fc region with two principal cell surface receptors, FcvarepsilonRI and CD23. Crosslinking of FcvarepsilonRI-bound IgE on mast cells and basophils by allergen initiates an immediate inflammatory response, while the interaction of IgE with CD23 on B-cells regulates IgE production. We have determined the structures of the C-type lectin "head" domain of CD23 from seven crystal forms. The thirty-five independent structures reveal extensive conformational plasticity in two loops that are critical for IgE binding.


==About this Structure==
Conformational plasticity at the IgE-binding site of the B-cell receptor CD23.,Dhaliwal B, Pang MO, Yuan D, Yahya N, Fabiane SM, McDonnell JM, Gould HJ, Beavil AJ, Sutton BJ Mol Immunol. 2013 Aug 6;56(4):693-697. doi: 10.1016/j.molimm.2013.07.005. PMID:23933509<ref>PMID:23933509</ref>
[[4j6m]] is a 8 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=4J6M OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<ref group="xtra">PMID:023933509</ref><references group="xtra"/><references/>
</div>
<div class="pdbe-citations 4j6m" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[CD23|CD23]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Dhaliwal, B.]]
[[Category: Large Structures]]
[[Category: Fabiane, S M.]]
[[Category: Dhaliwal B]]
[[Category: Sutton, B J.]]
[[Category: Fabiane SM]]
[[Category: Antibody receptor]]
[[Category: Sutton BJ]]
[[Category: Immune system]]
[[Category: Immunoglobulin fold lectin]]

Latest revision as of 18:37, 20 September 2023

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

Structural highlights

4j6m is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.48Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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).

Publication Abstract from PubMed

IgE antibodies play a central role in allergic disease. They recognize allergens via their Fab regions, whilst their effector functions are controlled through interactions of the Fc region with two principal cell surface receptors, FcvarepsilonRI and CD23. Crosslinking of FcvarepsilonRI-bound IgE on mast cells and basophils by allergen initiates an immediate inflammatory response, while the interaction of IgE with CD23 on B-cells regulates IgE production. We have determined the structures of the C-type lectin "head" domain of CD23 from seven crystal forms. The thirty-five independent structures reveal extensive conformational plasticity in two loops that are critical for IgE binding.

Conformational plasticity at the IgE-binding site of the B-cell receptor CD23.,Dhaliwal B, Pang MO, Yuan D, Yahya N, Fabiane SM, McDonnell JM, Gould HJ, Beavil AJ, Sutton BJ Mol Immunol. 2013 Aug 6;56(4):693-697. doi: 10.1016/j.molimm.2013.07.005. PMID:23933509[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. 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

4j6m, resolution 2.48Å

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