2ovu

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[[Image:2ovu.jpg|left|200px]]<br /><applet load="2ovu" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ovu.jpg|left|200px]]
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caption="2ovu, resolution 1.50&Aring;" />
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'''Crystal strucure of a lectin from Canavalia gladiata (CGL) in complex with man1-2man-OMe'''<br />
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{{Structure
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|PDB= 2ovu |SIZE=350|CAPTION= <scene name='initialview01'>2ovu</scene>, resolution 1.50&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''Crystal strucure of a lectin from Canavalia gladiata (CGL) in complex with man1-2man-OMe'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2OVU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Canavalia_gladiata Canavalia gladiata] with <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=2OVU OCA].
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2OVU is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Canavalia_gladiata Canavalia gladiata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OVU OCA].
==Reference==
==Reference==
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Structural analysis of Canavalia maritima and Canavalia gladiata lectins complexed with different dimannosides: new insights into the understanding of the structure-biological activity relationship in legume lectins., Bezerra GA, Oliveira TM, Moreno FB, de Souza EP, da Rocha BA, Benevides RG, Delatorre P, de Azevedo WF Jr, Cavada BS, J Struct Biol. 2007 Nov;160(2):168-76. Epub 2007 Aug 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17881248 17881248]
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Structural analysis of Canavalia maritima and Canavalia gladiata lectins complexed with different dimannosides: new insights into the understanding of the structure-biological activity relationship in legume lectins., Bezerra GA, Oliveira TM, Moreno FB, de Souza EP, da Rocha BA, Benevides RG, Delatorre P, de Azevedo WF Jr, Cavada BS, J Struct Biol. 2007 Nov;160(2):168-76. Epub 2007 Aug 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17881248 17881248]
[[Category: Canavalia gladiata]]
[[Category: Canavalia gladiata]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: sugar binding protein]]
[[Category: sugar binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:23:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:05:10 2008''

Revision as of 16:05, 20 March 2008


PDB ID 2ovu

Drag the structure with the mouse to rotate
, resolution 1.50Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



Crystal strucure of a lectin from Canavalia gladiata (CGL) in complex with man1-2man-OMe


Overview

Plant lectins, especially those purified from species of the Leguminosae family, represent the best studied group of carbohydrate-binding proteins. The legume lectins from Diocleinae subtribe are highly similar proteins that present significant differences in the potency/efficacy of their biological activities. The structural studies of the interactions between lectins and sugars may clarify the origin of the distinct biological activities observed in this high similar class of proteins. In this way, this work presents a crystallographic study of the ConM and CGL (agglutinins from Canavalia maritima and Canavalia gladiata, respectively) in the following complexes: ConM/CGL:Man(alpha1-2)Man(alpha1-O)Me, ConM/CGL:Man(alpha1-3)Man(alpha1-O)Me and ConM/CGL:Man(alpha1-4)Man(alpha1-O)Me, which crystallized in different conditions and space group from the native proteins. The structures were solved by molecular replacement, presenting satisfactory values for R(factor) and R(free). Comparisons between ConM, CGL and ConA (Canavalia ensiformis lectin) binding mode with the dimannosides in subject, presented different interactions patterns, which may account for a structural explanation of the distincts biological properties observed in the lectins of Diocleinae subtribe.

About this Structure

2OVU is a Protein complex structure of sequences from Canavalia gladiata. Full crystallographic information is available from OCA.

Reference

Structural analysis of Canavalia maritima and Canavalia gladiata lectins complexed with different dimannosides: new insights into the understanding of the structure-biological activity relationship in legume lectins., Bezerra GA, Oliveira TM, Moreno FB, de Souza EP, da Rocha BA, Benevides RG, Delatorre P, de Azevedo WF Jr, Cavada BS, J Struct Biol. 2007 Nov;160(2):168-76. Epub 2007 Aug 16. PMID:17881248

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