1dqo

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(New page: 200px<br /><applet load="1dqo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dqo, resolution 2.2&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[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;" />
caption="1dqo, resolution 2.2&Aring;" />
'''CRYSTAL STRUCTURE OF THE CYSTEINE RICH DOMAIN OF MANNOSE RECEPTOR COMPLEXED WITH ACETYLGALACTOSAMINE-4-SULFATE'''<br />
'''CRYSTAL STRUCTURE OF THE CYSTEINE RICH DOMAIN OF MANNOSE RECEPTOR COMPLEXED WITH ACETYLGALACTOSAMINE-4-SULFATE'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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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].
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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==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bjorkman, P.J.]]
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[[Category: Bjorkman, P J.]]
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[[Category: Chirino, A.J.]]
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[[Category: Chirino, A J.]]
[[Category: Feizi, T.]]
[[Category: Feizi, T.]]
[[Category: Leteux, C.]]
[[Category: Leteux, C.]]
[[Category: Liu, Y.]]
[[Category: Liu, Y.]]
[[Category: Misulovin, Z.]]
[[Category: Misulovin, Z.]]
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[[Category: Nussenzweig, M.C.]]
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[[Category: Nussenzweig, M C.]]
[[Category: ASG]]
[[Category: ASG]]
[[Category: beta trefoil]]
[[Category: beta trefoil]]
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[[Category: sulfated carbohydrate]]
[[Category: sulfated carbohydrate]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:30:03 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:28 2008''

Revision as of 10:19, 21 February 2008


1dqo, resolution 2.2Å

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CRYSTAL STRUCTURE OF THE CYSTEINE RICH DOMAIN OF MANNOSE RECEPTOR COMPLEXED WITH ACETYLGALACTOSAMINE-4-SULFATE

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.

About this Structure

1DQO is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the cysteine-rich domain of mannose receptor complexed with a sulfated carbohydrate ligand., Liu Y, Chirino AJ, Misulovin Z, Leteux C, Feizi T, Nussenzweig MC, Bjorkman PJ, J Exp Med. 2000 Apr 3;191(7):1105-16. PMID:10748229

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