1hli: Difference between revisions
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{{Theoretical_model}} | |||
==MODELING OF THE LECTIN-HOMOLOGY DOMAINS OF THE HUMAN AND MURINE LOW-AFFINITY FCE RECEPTOR (FCERII(SLASH)CD23)== | ==MODELING OF THE LECTIN-HOMOLOGY DOMAINS OF THE HUMAN AND MURINE LOW-AFFINITY FCE RECEPTOR (FCERII(SLASH)CD23)== | ||
<StructureSection load='1hli' size='340' side='right' caption='[[1hli]]' scene=''> | <StructureSection load='1hli' size='340' side='right' caption='[[1hli]]' scene=''> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Theoretical Model]] | |||
[[Category: Helm, B A]] | [[Category: Helm, B A]] | ||
[[Category: Padlan, E A]] | [[Category: Padlan, E A]] | ||
Revision as of 12:00, 11 February 2016
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MODELING OF THE LECTIN-HOMOLOGY DOMAINS OF THE HUMAN AND MURINE LOW-AFFINITY FCE RECEPTOR (FCERII(SLASH)CD23)MODELING OF THE LECTIN-HOMOLOGY DOMAINS OF THE HUMAN AND MURINE LOW-AFFINITY 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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