Modeling of the lectin-homology domains of the human and murine low-affinity Fc epsilon receptor (Fc epsilon RII/CD23).
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.
Padlan
E A
EA
Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
Helm
B A
BA
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry; D003198:Computer Simulation; D006801:Humans; D037102:Lectins / Q000737:chemistry*; D037241:Mannose-Binding Lectins; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D051381:Rats; D011961:Receptors, Fc / Q000737:chemistry*; D017455:Receptors, IgE / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D002352:Carrier Proteins; D037102:Lectins; D037241:Mannose-Binding Lectins; D011961:Receptors, Fc; D017455:Receptors, IgE