1hlj: Difference between revisions

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{{Theoretical_model}}
{{Theoretical_model}}


[[Image:1hlj.png|left|200px]]
==MODELING OF THE LECTIN-HOMOLOGY DOMAINS OF THE HUMAN AND MURINE FCE RECEPTOR (FCERII(SLASH)CD23)==
<StructureSection load='1hlj' size='340' side='right'caption='[[1hlj]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HLJ FirstGlance]. <br>
</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=1hlj FirstGlance], [https://www.ebi.ac.uk/pdbsum/1hlj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hlj ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Models of the lectin-homology domains of the human and murine low-affinity receptors for IgE (Fc epsilon RII/CD23) were built on the basis of sequence similarity with rat mannose-binding protein, the structure of which is known. The sites on Fc epsilon RII/CD23 that are possibly involved in the interaction with IgE and with another ligand, CD21/CR2, are proposed. The models may assist the design of protein engineering experiments for the study of the reactivity of these molecules.


{{STRUCTURE_1hlj|  PDB=1hlj  |  SCENE=  }}
Modeling of the lectin-homology domains of the human and murine low-affinity Fc epsilon receptor (Fc epsilon RII/CD23).,Padlan EA, Helm BA Receptor. 1993 Winter;3(4):325-41. PMID:8142907<ref>PMID:8142907</ref>


===MODELING OF THE LECTIN-HOMOLOGY DOMAINS OF THE HUMAN AND MURINE FCE RECEPTOR (FCERII(SLASH)CD23)===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_8142907}}
<div class="pdbe-citations 1hlj" style="background-color:#fffaf0;"></div>
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:008142907</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Theoretical Model]]
[[Category: Large Structures]]
[[Category: Helm, B A]]
[[Category: Helm, B A]]
[[Category: Padlan, E A]]
[[Category: Padlan, E A]]

Latest revision as of 13:50, 4 August 2021

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

MODELING OF THE LECTIN-HOMOLOGY DOMAINS OF THE HUMAN AND MURINE FCE RECEPTOR (FCERII(SLASH)CD23)MODELING OF THE LECTIN-HOMOLOGY DOMAINS OF THE HUMAN AND MURINE FCE RECEPTOR (FCERII(SLASH)CD23)

Structural highlights

For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, PDBsum, ProSAT

Publication Abstract from PubMed

Models of the lectin-homology domains of the human and murine low-affinity receptors for IgE (Fc epsilon RII/CD23) were built on the basis of sequence similarity with rat mannose-binding protein, the structure of which is known. The sites on Fc epsilon RII/CD23 that are possibly involved in the interaction with IgE and with another ligand, CD21/CR2, are proposed. The models may assist the design of protein engineering experiments for the study of the reactivity of these molecules.

Modeling of the lectin-homology domains of the human and murine low-affinity Fc epsilon receptor (Fc epsilon RII/CD23).,Padlan EA, Helm BA Receptor. 1993 Winter;3(4):325-41. PMID:8142907[1]

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

References

  1. Padlan EA, Helm BA. Modeling of the lectin-homology domains of the human and murine low-affinity Fc epsilon receptor (Fc epsilon RII/CD23). Receptor. 1993 Winter;3(4):325-41. PMID:8142907
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