2cyf

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(New page: 200px<br /><applet load="2cyf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cyf, resolution 1.80&Aring;" /> '''The Crystal Structur...)
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[[Image:2cyf.gif|left|200px]]<br /><applet load="2cyf" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2cyf.gif|left|200px]]<br /><applet load="2cyf" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2cyf, resolution 1.80&Aring;" />
caption="2cyf, resolution 1.80&Aring;" />
'''The Crystal Structure of Canavalia Maritima Lectin (ConM) in Complex with Trehalose and Maltose'''<br />
'''The Crystal Structure of Canavalia Maritima Lectin (ConM) in Complex with Trehalose and Maltose'''<br />
==Overview==
==Overview==
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The crystal structure of Canavalia maritima lectin (ConM) complexed with, trehalose and maltose revealed relevant point mutations in ConA-like, lectins. ConM with the disaccharides and other ConA-like lectins complexed, with carbohydrates demonstrated significant differences in the position of, H-bonds. The main difference in the ConM structure is the replacement of, Pro202 by Ser202, a residue that promotes the approximation of Tyr12 to, the carbohydrate-binding site. The O-6' of the second glucose ring in, maltose interacts with Tyr12, while in trehalose the interaction is, established by the O-2' and Tyr12, explaining the higher affinity of ConM, for disaccharides compared to monosaccharides.
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The crystal structure of Canavalia maritima lectin (ConM) complexed with trehalose and maltose revealed relevant point mutations in ConA-like lectins. ConM with the disaccharides and other ConA-like lectins complexed with carbohydrates demonstrated significant differences in the position of H-bonds. The main difference in the ConM structure is the replacement of Pro202 by Ser202, a residue that promotes the approximation of Tyr12 to the carbohydrate-binding site. The O-6' of the second glucose ring in maltose interacts with Tyr12, while in trehalose the interaction is established by the O-2' and Tyr12, explaining the higher affinity of ConM for disaccharides compared to monosaccharides.
==About this Structure==
==About this Structure==
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2CYF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Canavalia_maritima Canavalia maritima] with MAL, CA and MN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CYF OCA].
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2CYF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Canavalia_maritima Canavalia maritima] with <scene name='pdbligand=MAL:'>MAL</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYF OCA].
==Reference==
==Reference==
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[[Category: Canavalia maritima]]
[[Category: Canavalia maritima]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Cavada, B.S.]]
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[[Category: Cavada, B S.]]
[[Category: Delatorre, P.]]
[[Category: Delatorre, P.]]
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[[Category: Gadelha, C.A.A.]]
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[[Category: Gadelha, C A.A.]]
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[[Category: Jr., W.F.Azevedo.]]
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[[Category: Jr., W F.Azevedo.]]
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[[Category: Rocha, B.A.M.]]
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[[Category: Rocha, B A.M.]]
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[[Category: Sousa, E.P.]]
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[[Category: Sousa, E P.]]
[[Category: CA]]
[[Category: CA]]
[[Category: MAL]]
[[Category: MAL]]
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[[Category: maltose]]
[[Category: maltose]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:20:43 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:53:41 2008''

Revision as of 14:53, 21 February 2008


2cyf, resolution 1.80Å

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The Crystal Structure of Canavalia Maritima Lectin (ConM) in Complex with Trehalose and Maltose

Overview

The crystal structure of Canavalia maritima lectin (ConM) complexed with trehalose and maltose revealed relevant point mutations in ConA-like lectins. ConM with the disaccharides and other ConA-like lectins complexed with carbohydrates demonstrated significant differences in the position of H-bonds. The main difference in the ConM structure is the replacement of Pro202 by Ser202, a residue that promotes the approximation of Tyr12 to the carbohydrate-binding site. The O-6' of the second glucose ring in maltose interacts with Tyr12, while in trehalose the interaction is established by the O-2' and Tyr12, explaining the higher affinity of ConM for disaccharides compared to monosaccharides.

About this Structure

2CYF is a Protein complex structure of sequences from Canavalia maritima with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of a lectin from Canavalia maritima (ConM) in complex with trehalose and maltose reveals relevant mutation in ConA-like lectins., Delatorre P, Rocha BA, Gadelha CA, Santi-Gadelha T, Cajazeiras JB, Souza EP, Nascimento KS, Freire VN, Sampaio AH, Azevedo WF Jr, Cavada BS, J Struct Biol. 2006 Jun;154(3):280-6. Epub 2006 Apr 21. PMID:16677825

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