2cy6: Difference between revisions
New page: left|200px<br /><applet load="2cy6" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cy6, resolution 2.00Å" /> '''Crystal structure of... |
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[[Image:2cy6.gif|left|200px]]<br /><applet load="2cy6" size=" | [[Image:2cy6.gif|left|200px]]<br /><applet load="2cy6" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2cy6, resolution 2.00Å" /> | caption="2cy6, resolution 2.00Å" /> | ||
'''Crystal structure of ConM in complex with trehalose and maltose'''<br /> | '''Crystal structure of ConM in complex with trehalose and maltose'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of Canavalia maritima lectin (ConM) complexed with | 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== | ||
2CY6 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 CA, MN and TRE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 2CY6 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=CA:'>CA</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=TRE:'>TRE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CY6 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Canavalia maritima]] | [[Category: Canavalia maritima]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Cavada, B | [[Category: Cavada, B S.]] | ||
[[Category: Delatorre, P.]] | [[Category: Delatorre, P.]] | ||
[[Category: Gadelha, C | [[Category: Gadelha, C A.A.]] | ||
[[Category: Jr., W | [[Category: Jr., W F.Azevedo.]] | ||
[[Category: Rocha, B | [[Category: Rocha, B A.M.]] | ||
[[Category: Souza, E | [[Category: Souza, E P.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: MN]] | [[Category: MN]] | ||
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[[Category: x-ray diffraction]] | [[Category: x-ray diffraction]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:53:34 2008'' | ||
Revision as of 17:53, 21 February 2008
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Crystal structure of ConM in complex with trehalose and maltose
OverviewOverview
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 StructureAbout this Structure
2CY6 is a Protein complex structure of sequences from Canavalia maritima with , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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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