1azd: Difference between revisions
New page: left|200px<br /><applet load="1azd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1azd, resolution 3.0Å" /> '''CONCANAVALIN FROM CAN... |
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[[Image:1azd.jpg|left|200px]]<br /><applet load="1azd" size=" | [[Image:1azd.jpg|left|200px]]<br /><applet load="1azd" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1azd, resolution 3.0Å" /> | caption="1azd, resolution 3.0Å" /> | ||
'''CONCANAVALIN FROM CANAVALIA BRASILIENSIS'''<br /> | '''CONCANAVALIN FROM CANAVALIA BRASILIENSIS'''<br /> | ||
==Overview== | ==Overview== | ||
Canavalia brasiliensis lectin was isolated from the seeds of a Brazilian | 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== | ==About this Structure== | ||
1AZD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_brasiliensis Canavalia brasiliensis] with CA and MN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1AZD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_brasiliensis Canavalia brasiliensis] 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=1AZD OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Canavalia brasiliensis]] | [[Category: Canavalia brasiliensis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Calvete, J | [[Category: Calvete, J J.]] | ||
[[Category: Cavada, B | [[Category: Cavada, B S.]] | ||
[[Category: Grangeiro, T | [[Category: Grangeiro, T B.]] | ||
[[Category: Hermoso, J.]] | [[Category: Hermoso, J.]] | ||
[[Category: Sanz-Aparicio, J.]] | [[Category: Sanz-Aparicio, J.]] | ||
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[[Category: legume lectin]] | [[Category: legume lectin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:49:51 2008'' | ||
Revision as of 12:49, 21 February 2008
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CONCANAVALIN FROM CANAVALIA BRASILIENSIS
OverviewOverview
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 StructureAbout this Structure
1AZD is a Single protein structure of sequence from Canavalia brasiliensis with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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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