User:Anthony Davis/Sandbox1 IgE: Difference between revisions

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=Structure=

The FcεRI receptor is a tetrameric receptor complex consisting of one alpha, one beta, and two disulfide bridge connected gamma chains.[http://upload.wikimedia.org/wikipedia/commons/4/42/Fc%CE%B5RI_Receptor.jpg]. The alpha subunit is the one dedicated to the binding of IgE.

The structure of the FcϵRI alpha subunit is made up of two (Ig)domains <scene name='User:Anthony_Davis/Sandbox1_IgE/D2_d1/2'>D2 and D1</scene. The domains form a convex shape at the top of the receptor that is directly involved in binding IgE. Another feature of the FcϵRI alpha subunit is the <scene name='User:Anthony_Davis/Sandbox1_IgE/Fg_loop/1'>FG Loop</scene> which forms part of the binding site for IgE.

The structure of the FcϵRI alpha subunit is made up of two (Ig)domains <scene name='User:Anthony_Davis/Sandbox1_IgE/D2_d1/2'>D2 and D1</scene>. The domains form a convex shape at the top of the receptor that is directly involved in binding IgE. Another feature of the FcϵRI alpha subunit is the <scene name='User:Anthony_Davis/Sandbox1_IgE/Fg_loop/1'>FG Loop</scene> which forms part of the binding site for IgE.

The FcεRI residues that have been implicated in IgE binding include residues numbers <scene name='User:Anthony_Davis/Sandbox1_IgE/Ige_binding_residues/1'>115, 117, 118</scene>, and <scene name='User:Anthony_Davis/Sandbox1_IgE/Ige_binding_residues/3'>120,121,122 and 123</scene> in the D2 C strand , <scene name='User:Anthony_Davis/Sandbox1_IgE/Ige_binding_residue/1'>129 and 131</scene> in the C′-E loop , <scene name='User:Anthony_Davis/Sandbox1_IgE/Ige_binding_residues/5'>149 and 153</scene> the F strand, <scene name='User:Anthony_Davis/Sandbox1_IgE/Ige_binding_residues/6'>155</scene> in the FG loop, and <scene name='User:Anthony_Davis/Sandbox1_IgE/Ige_binding_residues/7'>159</scene> in the G strand. In addition, residues 87 at the D1D2 interface and 128 in the C′-E loop are likely to be part of the IgE interaction site, since mutation of these residues influences receptor binding to IgE.

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 =Structure=
 The FcεRI receptor is a tetrameric receptor complex consisting of one alpha, one beta, and two disulfide bridge connected gamma chains.[http://upload.wikimedia.org/wikipedia/commons/4/42/Fc%CE%B5RI_Receptor.jpg]. The alpha subunit is the one dedicated to the binding of IgE.
-The structure of the FcϵRI alpha subunit is made up of two (Ig)domains <scene name='User:Anthony_Davis/Sandbox1_IgE/D2_d1/2'>D2 and D1</scene. The domains form a convex shape at the top of the receptor that is directly involved in binding IgE. Another feature of the FcϵRI alpha subunit is the <scene name='User:Anthony_Davis/Sandbox1_IgE/Fg_loop/1'>FG Loop</scene> which forms part of the binding site for IgE.
+The structure of the FcϵRI alpha subunit is made up of two (Ig)domains <scene name='User:Anthony_Davis/Sandbox1_IgE/D2_d1/2'>D2 and D1</scene>. The domains form a convex shape at the top of the receptor that is directly involved in binding IgE. Another feature of the FcϵRI alpha subunit is the <scene name='User:Anthony_Davis/Sandbox1_IgE/Fg_loop/1'>FG Loop</scene> which forms part of the binding site for IgE.
 The FcεRI residues that have been implicated in IgE binding include residues numbers <scene name='User:Anthony_Davis/Sandbox1_IgE/Ige_binding_residues/1'>115, 117, 118</scene>, and <scene name='User:Anthony_Davis/Sandbox1_IgE/Ige_binding_residues/3'>120,121,122 and 123</scene> in the D2 C strand , <scene name='User:Anthony_Davis/Sandbox1_IgE/Ige_binding_residue/1'>129 and 131</scene> in the C′-E loop , <scene name='User:Anthony_Davis/Sandbox1_IgE/Ige_binding_residues/5'>149 and 153</scene> the F strand, <scene name='User:Anthony_Davis/Sandbox1_IgE/Ige_binding_residues/6'>155</scene> in the FG loop, and  <scene name='User:Anthony_Davis/Sandbox1_IgE/Ige_binding_residues/7'>159</scene> in the G strand. In addition, residues 87 at the D1D2 interface and 128 in the C′-E loop are likely to be part of the IgE interaction site, since mutation of these residues influences receptor binding to IgE.