1hlj: Difference between revisions
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{{Theoretical_model}} | {{Theoretical_model}} | ||
[[ | ==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. | |||
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> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 1hlj" style="background-color:#fffaf0;"></div> | |||
== References == | |||
== | <references/> | ||
< | __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
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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
Publication Abstract from PubMedModels 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 |
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