1azd
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1azd.jpg|left|200px]] | + | [[Image:1azd.jpg|left|200px]] |
| - | + | ||
| - | '''CONCANAVALIN FROM CANAVALIA BRASILIENSIS''' | + | {{Structure |
| + | |PDB= 1azd |SIZE=350|CAPTION= <scene name='initialview01'>1azd</scene>, resolution 3.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CONCANAVALIN FROM CANAVALIA BRASILIENSIS''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1AZD is a [ | + | 1AZD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_brasiliensis Canavalia brasiliensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AZD OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9094437 9094437] |
[[Category: Canavalia brasiliensis]] | [[Category: Canavalia brasiliensis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 22: | Line 31: | ||
[[Category: legume lectin]] | [[Category: legume lectin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:04:19 2008'' |
Revision as of 08:04, 20 March 2008
| |||||||
| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| 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
Page seeded by OCA on Thu Mar 20 10:04:19 2008
