1azd

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|PDB= 1azd |SIZE=350|CAPTION= <scene name='initialview01'>1azd</scene>, resolution 3.0&Aring;
|PDB= 1azd |SIZE=350|CAPTION= <scene name='initialview01'>1azd</scene>, resolution 3.0&Aring;
|SITE=
|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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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1azd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1azd OCA], [http://www.ebi.ac.uk/pdbsum/1azd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1azd RCSB]</span>
}}
}}
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[[Category: Hermoso, J.]]
[[Category: Hermoso, J.]]
[[Category: Sanz-Aparicio, J.]]
[[Category: Sanz-Aparicio, J.]]
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[[Category: CA]]
 
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[[Category: MN]]
 
[[Category: legume lectin]]
[[Category: legume lectin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:04:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:50:34 2008''

Revision as of 15:50, 30 March 2008


PDB ID 1azd

Drag the structure with the mouse to rotate
, resolution 3.0Å
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CONCANAVALIN FROM CANAVALIA BRASILIENSIS


Overview

Canavalia brasiliensis lectin was isolated from the seeds of a Brazilian autochthonous Leguminosae plant. Despite extensive amino acid sequence similarity with Concanavalin A, C. brasiliensis lectin exerts in vitro and in vivo cellular effects that are markedly different from those displayed by Concanavalin A. We have solved the crystal structure of the C. brasiliensis lectin at 3.0 A resolution. The three-dimensional structure of the lectin monomer can be superimposed onto that of Concanavalin A with a root-mean-square deviation for all C alpha atoms of 0.65 A. However, this parameter is 0.84 and 1.62 A when the C. brasiliensis lectin dimer and tetramer, respectively, are compared with the same structures of Concanavalin A. We suggest that these differences in quaternary structure may account for the different biological properties of these two highly related Leguminosae lectins.

About this Structure

1AZD is a Single protein structure of sequence from Canavalia brasiliensis. Full crystallographic information is available from OCA.

Reference

The crystal structure of Canavalia brasiliensis lectin suggests a correlation between its quaternary conformation and its distinct biological properties from Concanavalin A., Sanz-Aparicio J, Hermoso J, Grangeiro TB, Calvete JJ, Cavada BS, FEBS Lett. 1997 Mar 17;405(1):114-8. PMID:9094437

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