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1fwv

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[[Image:1fwv.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1fwv| PDB=1fwv | SCENE= }}
{{STRUCTURE_1fwv| PDB=1fwv | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF MANNOSE RECEPTOR COMPLEXED WITH 3-SO4-LEWIS(A)'''
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===CRYSTAL STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF MANNOSE RECEPTOR COMPLEXED WITH 3-SO4-LEWIS(A)===
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==Overview==
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The mannose receptor (MR) binds foreign and host ligands through interactions with their carbohydrates. Two portions of MR have distinct carbohydrate recognition properties. One is conferred by the amino-terminal cysteine-rich domain (Cys-MR), which plays a critical role in binding sulfated glycoproteins including pituitary hormones. The other is achieved by tandemly arranged C-type lectin domains that facilitate carbohydrate-dependent uptake of infectious microorganisms. This dual carbohydrate binding specificity enables MR to bind ligands by interacting with both sulfated and non-sulfated polysaccharide chains. We previously determined crystal structures of Cys-MR complexed with 4-SO(4)-N-acetylglucosamine and with an unidentified ligand resembling Hepes (N-[2-hydroxyethyl]piperazine-N'-[2-ethanesulfonic acid]). In continued efforts to elucidate the mechanism of sulfated carbohydrate recognition by Cys-MR, we characterized the binding affinities between Cys-MR and potential carbohydrate ligands using a fluorescence-based assay. We find that Cys-MR binds sulfated carbohydrates with relatively high affinities (K(D)=0.1 mM to 1.0 mM) compared to the affinities of other lectins. Cys-MR also binds Hepes with a K(D) value of 3.9 mM, consistent with the suggestion that the ligand in the original Cys-MR crystal structure is Hepes. We also determined crystal structures of Cys-MR complexed with 3-SO(4)-Lewis(x), 3-SO(4)-Lewis(a), and 6-SO(4)-N-acetylglucosamine at 1.9 A, 2.2 A, and 2.5 A resolution, respectively, and the 2.0 A structure of Cys-MR that had been treated to remove Hepes. The conformation of the Cys-MR binding site is virtually identical in all Cys-MR crystal structures, suggesting that Cys-MR does not undergo conformational changes upon ligand binding. The structures are used to rationalize the binding affinities derived from the biochemical studies and to elucidate the molecular mechanism of sulfated carbohydrate recognition by Cys-MR.
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(as it appears on PubMed at http://www.pubmed.gov), where 11152606 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11152606}}
==About this Structure==
==About this Structure==
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[[Category: Mannose receptor]]
[[Category: Mannose receptor]]
[[Category: Sulfated carbohydrate]]
[[Category: Sulfated carbohydrate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:51:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:03:54 2008''

Revision as of 01:03, 1 July 2008

Image:1fwv.png

Template:STRUCTURE 1fwv

CRYSTAL STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF MANNOSE RECEPTOR COMPLEXED WITH 3-SO4-LEWIS(A)

Template:ABSTRACT PUBMED 11152606

About this Structure

1FWV is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

The molecular mechanism of sulfated carbohydrate recognition by the cysteine-rich domain of mannose receptor., Liu Y, Misulovin Z, Bjorkman PJ, J Mol Biol. 2001 Jan 19;305(3):481-90. PMID:11152606

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