1ouw

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(New page: 200px<br /><applet load="1ouw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ouw, resolution 1.37&Aring;" /> '''Crystal structure of...)
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[[Image:1ouw.gif|left|200px]]<br /><applet load="1ouw" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ouw.gif|left|200px]]<br /><applet load="1ouw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ouw, resolution 1.37&Aring;" />
caption="1ouw, resolution 1.37&Aring;" />
'''Crystal structure of Calystegia sepium agglutinin'''<br />
'''Crystal structure of Calystegia sepium agglutinin'''<br />
==Overview==
==Overview==
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The high number of quaternary structures observed for lectins highlights, the important role of these oligomeric assemblies during carbohydrate, recognition events. Although a large diversity in the mode of association, of lectin subunits is frequently observed, the oligomeric assemblies of, plant lectins display small variations within a single family. The crystal, structure of the mannose-binding jacalin-related lectin from Calystegia, sepium (Calsepa) has been determined at 1.37-A resolution. Calsepa, exhibits the same beta-prism fold as identified previously for other, members of the family, but the shape and the hydrophobic character of its, carbohydrate-binding site is unlike that of other members, consistent with, surface plasmon resonance analysis showing a preference for methylated, sugars. Calsepa reveals a novel dimeric assembly markedly dissimilar to, those described earlier for Heltuba and jacalin but mimics the canonical, 12-stranded beta-sandwich dimer found in legume lectins. The present, structure exemplifies the adaptability of the beta-prism building block in, the evolution of plant lectins and highlights the biological role of these, quaternary structures for carbohydrate recognition.
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The high number of quaternary structures observed for lectins highlights the important role of these oligomeric assemblies during carbohydrate recognition events. Although a large diversity in the mode of association of lectin subunits is frequently observed, the oligomeric assemblies of plant lectins display small variations within a single family. The crystal structure of the mannose-binding jacalin-related lectin from Calystegia sepium (Calsepa) has been determined at 1.37-A resolution. Calsepa exhibits the same beta-prism fold as identified previously for other members of the family, but the shape and the hydrophobic character of its carbohydrate-binding site is unlike that of other members, consistent with surface plasmon resonance analysis showing a preference for methylated sugars. Calsepa reveals a novel dimeric assembly markedly dissimilar to those described earlier for Heltuba and jacalin but mimics the canonical 12-stranded beta-sandwich dimer found in legume lectins. The present structure exemplifies the adaptability of the beta-prism building block in the evolution of plant lectins and highlights the biological role of these quaternary structures for carbohydrate recognition.
==About this Structure==
==About this Structure==
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1OUW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Calystegia_sepium Calystegia sepium] with MLT, EDO and IMD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OUW OCA].
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1OUW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Calystegia_sepium Calystegia sepium] with <scene name='pdbligand=MLT:'>MLT</scene>, <scene name='pdbligand=EDO:'>EDO</scene> and <scene name='pdbligand=IMD:'>IMD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OUW OCA].
==Reference==
==Reference==
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[[Category: Calystegia sepium]]
[[Category: Calystegia sepium]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Astoul, C.H.]]
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[[Category: Astoul, C H.]]
[[Category: Barre, A.]]
[[Category: Barre, A.]]
[[Category: Bourne, Y.]]
[[Category: Bourne, Y.]]
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[[Category: Damme, E.J.M.van.]]
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[[Category: Damme, E J.M van.]]
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[[Category: Peumans, W.J.]]
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[[Category: Peumans, W J.]]
[[Category: Roig-Zamboni, V.]]
[[Category: Roig-Zamboni, V.]]
[[Category: Rouge, P.]]
[[Category: Rouge, P.]]
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[[Category: mannose-binding]]
[[Category: mannose-binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:28:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:55 2008''

Revision as of 12:21, 21 February 2008


1ouw, resolution 1.37Å

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Crystal structure of Calystegia sepium agglutinin

Overview

The high number of quaternary structures observed for lectins highlights the important role of these oligomeric assemblies during carbohydrate recognition events. Although a large diversity in the mode of association of lectin subunits is frequently observed, the oligomeric assemblies of plant lectins display small variations within a single family. The crystal structure of the mannose-binding jacalin-related lectin from Calystegia sepium (Calsepa) has been determined at 1.37-A resolution. Calsepa exhibits the same beta-prism fold as identified previously for other members of the family, but the shape and the hydrophobic character of its carbohydrate-binding site is unlike that of other members, consistent with surface plasmon resonance analysis showing a preference for methylated sugars. Calsepa reveals a novel dimeric assembly markedly dissimilar to those described earlier for Heltuba and jacalin but mimics the canonical 12-stranded beta-sandwich dimer found in legume lectins. The present structure exemplifies the adaptability of the beta-prism building block in the evolution of plant lectins and highlights the biological role of these quaternary structures for carbohydrate recognition.

About this Structure

1OUW is a Single protein structure of sequence from Calystegia sepium with , and as ligands. Full crystallographic information is available from OCA.

Reference

The crystal structure of the Calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a beta-prism fold., Bourne Y, Roig-Zamboni V, Barre A, Peumans WJ, Astoul CH, Van Damme EJ, Rouge P, J Biol Chem. 2004 Jan 2;279(1):527-33. Epub 2003 Oct 15. PMID:14561768

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