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{{Theoretical_model}}
{{Theoretical_model}}
{{Seed}}
[[Image:1kje.png|left|200px]]


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==THEORETICAL MODEL OF THE HUMAN CELL SURFACE RECEPTOR CD23, EXTRACELLULAR C-TYPE LECTIN DOMAIN, RESIDUES 178-285==
The line below this paragraph, containing "STRUCTURE_1kje", creates the "Structure Box" on the page.
<StructureSection load='1kje' size='340' side='right'caption='[[1kje]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KJE FirstGlance]. <br>
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</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=1kje FirstGlance], [https://www.ebi.ac.uk/pdbsum/1kje PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kje ProSAT]</span></td></tr>
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</table>
{{STRUCTURE_1kje|  PDB=1kje  |  SCENE=  }}
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CD23, a type II membrane receptor protein, recognizes four different ligands via its extracellular C-type lectin domain: immunoglobulin E (IgE), CD21, and the beta 2-integrins CD11b and CD11c. CD23 specifically interacts in a calcium-dependent manner, "lectin-like" with carbohydrate moieties expressed on CD21 and CD11b/c, but also "lectin-unlike" with protein epitopes on IgE. As a first step in analyzing the multiple binding specificities associated with CD23 in more detail, we report a detailed molecular model of the lectin-like domain of human CD23 (hCD23). The model was built based on information provided by X-ray structures of mannose binding protein (MBP) and E-selectin, both of which are members of the calcium-dependent (C-type) lectin superfamily. Sequence-structure comparisons suggest that hCD23 is structurally more similar to MBP than to E-selectin. The hCD23 model is compared to an independently derived model. Although the CD23-carbohydrate and CD23-protein interactions are both calcium dependent, analysis of the model suggests the presence of distinct binding sites for these ligands.


===THEORETICAL MODEL OF THE HUMAN CELL SURFACE RECEPTOR CD23, EXTRACELLULAR C-TYPE LECTIN DOMAIN, RESIDUES 178-285===
Structure-based modeling of the ligand binding domain of the human cell surface receptor CD23 and comparison of two independently derived molecular models.,Bajorath J, Aruffo A Protein Sci. 1996 Feb;5(2):240-7. PMID:8745401<ref>PMID:8745401</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_8745401}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1kje" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 8745401 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_8745401}}
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</StructureSection>
==About this Structure==
[[Category: Theoretical Model]]
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KJE OCA].
[[Category: Large Structures]]
 
==Reference==
<ref group="xtra">PMID:8745401</ref><references group="xtra"/>
[[Category: Bajorath, J]]
[[Category: Bajorath, J]]
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