1dqg

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(New page: 200px<br /><applet load="1dqg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dqg, resolution 1.7&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1dqg.gif|left|200px]]<br /><applet load="1dqg" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1dqg, resolution 1.7&Aring;" />
caption="1dqg, resolution 1.7&Aring;" />
'''CRYSTAL STRUCTURE OF THE CYSTEINE RICH DOMAIN OF MANNOSE RECEPTOR'''<br />
'''CRYSTAL STRUCTURE OF THE CYSTEINE RICH DOMAIN OF MANNOSE RECEPTOR'''<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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1DQG 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DQG OCA].
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1DQG 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQG 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: SO4]]
[[Category: SO4]]
[[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 13:29:51 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:21 2008''

Revision as of 10:19, 21 February 2008


1dqg, resolution 1.7Å

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CRYSTAL STRUCTURE OF THE CYSTEINE RICH DOMAIN OF MANNOSE RECEPTOR

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

1DQG 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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