1dqo: Difference between revisions

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[[Image:1dqo.gif|left|200px]]<br /><applet load="1dqo" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1dqo.gif|left|200px]]<br /><applet load="1dqo" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1dqo, resolution 2.2Å" />

'''CRYSTAL STRUCTURE OF THE CYSTEINE RICH DOMAIN OF MANNOSE RECEPTOR COMPLEXED WITH ACETYLGALACTOSAMINE-4-SULFATE'''<br />

==Overview==

The macrophage and epithelial cell mannose receptor (MR) binds, carbohydrates on foreign and host molecules. Two portions of MR recognize, carbohydrates: tandemly arranged C-type lectin domains facilitate, carbohydrate-dependent macrophage uptake of infectious organisms, and the, NH(2)-terminal cysteine-rich domain (Cys-MR) binds to sulfated, glycoproteins including pituitary hormones. To elucidate the mechanism of, sulfated carbohydrate recognition, we determined crystal structures of, Cys-MR alone and complexed with 4-sulfated-N-acetylgalactosamine at 1.7, and 2.2 A resolution, respectively. Cys-MR folds into an approximately, three-fold symmetric beta-trefoil shape resembling fibroblast growth, factor. The sulfate portions of 4-sulfated-N-acetylgalactosamine and an, unidentified ligand found in the native crystals bind in a neutral pocket, in the third lobe. We use the structures to rationalize the carbohydrate, binding specificities of Cys-MR and compare the recognition properties of, Cys-MR with other beta-trefoil proteins.

The macrophage and epithelial cell mannose receptor (MR) binds carbohydrates on foreign and host molecules. Two portions of MR recognize carbohydrates: tandemly arranged C-type lectin domains facilitate carbohydrate-dependent macrophage uptake of infectious organisms, and the NH(2)-terminal cysteine-rich domain (Cys-MR) binds to sulfated glycoproteins including pituitary hormones. To elucidate the mechanism of sulfated carbohydrate recognition, we determined crystal structures of Cys-MR alone and complexed with 4-sulfated-N-acetylgalactosamine at 1.7 and 2.2 A resolution, respectively. Cys-MR folds into an approximately three-fold symmetric beta-trefoil shape resembling fibroblast growth factor. The sulfate portions of 4-sulfated-N-acetylgalactosamine and an unidentified ligand found in the native crystals bind in a neutral pocket in the third lobe. We use the structures to rationalize the carbohydrate binding specificities of Cys-MR and compare the recognition properties of Cys-MR with other beta-trefoil proteins.

==About this Structure==

1DQO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ASG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1DQO OCA].

1DQO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ASG:'>ASG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQO OCA].

==Reference==

Line 13:

[[Category: Mus musculus]]

[[Category: Single protein]]

[[Category: Bjorkman, P.J.]]

[[Category: Bjorkman, P J.]]

[[Category: Chirino, A.J.]]

[[Category: Chirino, A J.]]

[[Category: Feizi, T.]]

[[Category: Leteux, C.]]

[[Category: Liu, Y.]]

[[Category: Misulovin, Z.]]

[[Category: Nussenzweig, M.C.]]

[[Category: Nussenzweig, M C.]]

[[Category: ASG]]

[[Category: beta trefoil]]

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[[Category: sulfated carbohydrate]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 13~~:30:~~03 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:28 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1dqo.gif|left|200px]]<br /><applet load="1dqo" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1dqo.gif|left|200px]]<br /><applet load="1dqo" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1dqo, resolution 2.2&Aring;" />
 '''CRYSTAL STRUCTURE OF THE CYSTEINE RICH DOMAIN OF MANNOSE RECEPTOR COMPLEXED WITH ACETYLGALACTOSAMINE-4-SULFATE'''<br />
 ==Overview==
-The macrophage and epithelial cell mannose receptor (MR) binds, carbohydrates on foreign and host molecules. Two portions of MR recognize, carbohydrates: tandemly arranged C-type lectin domains facilitate, carbohydrate-dependent macrophage uptake of infectious organisms, and the, NH(2)-terminal cysteine-rich domain (Cys-MR) binds to sulfated, glycoproteins including pituitary hormones. To elucidate the mechanism of, sulfated carbohydrate recognition, we determined crystal structures of, Cys-MR alone and complexed with 4-sulfated-N-acetylgalactosamine at 1.7, and 2.2 A resolution, respectively. Cys-MR folds into an approximately, three-fold symmetric beta-trefoil shape resembling fibroblast growth, factor. The sulfate portions of 4-sulfated-N-acetylgalactosamine and an, unidentified ligand found in the native crystals bind in a neutral pocket, in the third lobe. We use the structures to rationalize the carbohydrate, binding specificities of Cys-MR and compare the recognition properties of, Cys-MR with other beta-trefoil proteins.
+The macrophage and epithelial cell mannose receptor (MR) binds carbohydrates on foreign and host molecules. Two portions of MR recognize carbohydrates: tandemly arranged C-type lectin domains facilitate carbohydrate-dependent macrophage uptake of infectious organisms, and the NH(2)-terminal cysteine-rich domain (Cys-MR) binds to sulfated glycoproteins including pituitary hormones. To elucidate the mechanism of sulfated carbohydrate recognition, we determined crystal structures of Cys-MR alone and complexed with 4-sulfated-N-acetylgalactosamine at 1.7 and 2.2 A resolution, respectively. Cys-MR folds into an approximately three-fold symmetric beta-trefoil shape resembling fibroblast growth factor. The sulfate portions of 4-sulfated-N-acetylgalactosamine and an unidentified ligand found in the native crystals bind in a neutral pocket in the third lobe. We use the structures to rationalize the carbohydrate binding specificities of Cys-MR and compare the recognition properties of Cys-MR with other beta-trefoil proteins.
 ==About this Structure==
-DQO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ASG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DQO OCA].
+DQO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ASG:'>ASG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQO OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Mus musculus]]
 [[Category: Single protein]]
-[[Category: Bjorkman, P.J.]]
+[[Category: Bjorkman, P J.]]
-[[Category: Chirino, A.J.]]
+[[Category: Chirino, A J.]]
 [[Category: Feizi, T.]]
 [[Category: Leteux, C.]]
 [[Category: Liu, Y.]]
 [[Category: Misulovin, Z.]]
-[[Category: Nussenzweig, M.C.]]
+[[Category: Nussenzweig, M C.]]
 [[Category: ASG]]
 [[Category: beta trefoil]]
@@ Line 26: / Line 26: @@
 [[Category: sulfated carbohydrate]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:30:03 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:28 2008''