1t8d: Difference between revisions

Revision as of 16:10, 21 February 2008

Structure of the C-type lectin domain of CD23

OverviewOverview

The low-affinity immunoglobulin E (IgE) receptor, CD23 (FcepsilonRII), binds both IgE and CD21 and, through these interactions, regulates the synthesis of IgE, the antibody isotype that mediates the allergic response. We have determined the three-dimensional structure of the C-type lectin domain of CD23 in solution by nuclear magnetic resonance spectroscopy. An analysis of concentration-dependent chemical shift perturbations have allowed us to identify the residues engaged in self-association to the trimeric state, whereas ligand-induced changes have defined the binding sites for IgE and CD21. The results further reveal that CD23 can bind both ligands simultaneously. Despite the C-type lectin domain structure, none of the interactions require calcium. We also find that IgE and CD23 can interact to form high molecular mass multimeric complexes. The interactions that we have described provide a solution to the paradox that CD23 is involved in both up- and down-regulation of IgE and provide a structural basis for the development of inhibitors of allergic disease.

About this StructureAbout this Structure

1T8D is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

The structure of human CD23 and its interactions with IgE and CD21., Hibbert RG, Teriete P, Grundy GJ, Beavil RL, Reljic R, Holers VM, Hannan JP, Sutton BJ, Gould HJ, McDonnell JM, J Exp Med. 2005 Sep 19;202(6):751-60. PMID:16172256

Page seeded by OCA on Thu Feb 21 15:10:57 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1t8d.gif|left|200px]]<br />
+[[Image:1t8d.gif|left|200px]]<br /><applet load="1t8d" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1t8d" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1t8d" />
 '''Structure of the C-type lectin domain of CD23'''<br />
 ==Overview==
-The low-affinity immunoglobulin E (IgE) receptor, CD23 (FcepsilonRII), binds both IgE and CD21 and, through these interactions, regulates the, synthesis of IgE, the antibody isotype that mediates the allergic, response. We have determined the three-dimensional structure of the C-type, lectin domain of CD23 in solution by nuclear magnetic resonance, spectroscopy. An analysis of concentration-dependent chemical shift, perturbations have allowed us to identify the residues engaged in, self-association to the trimeric state, whereas ligand-induced changes, have defined the binding sites for IgE and CD21. The results further, reveal that CD23 can bind both ligands simultaneously. Despite the C-type, lectin domain structure, none of the interactions require calcium. We also, find that IgE and CD23 can interact to form high molecular mass multimeric, complexes. The interactions that we have described provide a solution to, the paradox that CD23 is involved in both up- and down-regulation of IgE, and provide a structural basis for the development of inhibitors of, allergic disease.
+The low-affinity immunoglobulin E (IgE) receptor, CD23 (FcepsilonRII), binds both IgE and CD21 and, through these interactions, regulates the synthesis of IgE, the antibody isotype that mediates the allergic response. We have determined the three-dimensional structure of the C-type lectin domain of CD23 in solution by nuclear magnetic resonance spectroscopy. An analysis of concentration-dependent chemical shift perturbations have allowed us to identify the residues engaged in self-association to the trimeric state, whereas ligand-induced changes have defined the binding sites for IgE and CD21. The results further reveal that CD23 can bind both ligands simultaneously. Despite the C-type lectin domain structure, none of the interactions require calcium. We also find that IgE and CD23 can interact to form high molecular mass multimeric complexes. The interactions that we have described provide a solution to the paradox that CD23 is involved in both up- and down-regulation of IgE and provide a structural basis for the development of inhibitors of allergic disease.
 ==About this Structure==
-T8D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T8D OCA].
+T8D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T8D OCA].
 ==Reference==
@@ Line 14: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Gould, H.J.]]
+[[Category: Gould, H J.]]
-[[Category: Grundy, G.J.]]
+[[Category: Grundy, G J.]]
-[[Category: Hibbert, R.G.]]
+[[Category: Hibbert, R G.]]
-[[Category: McDonnell, J.M.]]
+[[Category: McDonnell, J M.]]
-[[Category: Sutton, B.J.]]
+[[Category: Sutton, B J.]]
 [[Category: Teriete, P.]]
 [[Category: c-type lectin]]
@@ Line 25: / Line 24: @@
 [[Category: ige]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:22:02 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:57 2008''