2cwm: Difference between revisions
New page: left|200px<br /><applet load="2cwm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cwm, resolution 1.95Å" /> '''Native Crystal Struc... |
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[[Image:2cwm.gif|left|200px]]<br /><applet load="2cwm" size=" | [[Image:2cwm.gif|left|200px]]<br /><applet load="2cwm" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2cwm, resolution 1.95Å" /> | caption="2cwm, resolution 1.95Å" /> | ||
'''Native Crystal Structure of NO releasing inductive lectin from seeds of the Canavalia maritima (ConM)'''<br /> | '''Native Crystal Structure of NO releasing inductive lectin from seeds of the Canavalia maritima (ConM)'''<br /> | ||
==Overview== | ==Overview== | ||
Here, we report the crystallographic study of a lectin from Canavalia | Here, we report the crystallographic study of a lectin from Canavalia maritima seeds (ConM) and its relaxant activity on vascular smooth muscle, to provide new insights into the understanding of structure/function relationships of this class of proteins. ConM was crystallized and its structure determined by standard molecular replacement techniques. The amino acid residues, previously suggested incorrectly by manual sequencing, have now been determined as I17, I53, S129, S134, G144, S164, P165, S187, V190, S169, T196, and S202. Analysis of the structure indicated a dimer in the asymmetric unit, two metal binding sites per monomer, and loops involved in the molecular oligomerization. These confer 98% similarity between ConM and other previously described lectins, derived from Canavalia ensiformis and Canavalia brasiliensis. Our functional data indicate that ConM exerts a concentration-dependent relaxant action on isolated aortic rings that probably occurs via an interaction with a specific lectin-binding site on the endothelium, resulting in a release of nitric oxide. | ||
==About this Structure== | ==About this Structure== | ||
2CWM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Canavalia_maritima Canavalia maritima] with CA and MN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 2CWM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Canavalia_maritima Canavalia maritima] 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=2CWM OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Canavalia maritima]] | [[Category: Canavalia maritima]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Assreuy, A | [[Category: Assreuy, A M.S.]] | ||
[[Category: Cavada, B | [[Category: Cavada, B S.]] | ||
[[Category: Criddle, D | [[Category: Criddle, D N.]] | ||
[[Category: Delatorre, P.]] | [[Category: Delatorre, P.]] | ||
[[Category: Gadelha, C | [[Category: Gadelha, C A.A.]] | ||
[[Category: Jr., W | [[Category: Jr., W F.De Azevedo.]] | ||
[[Category: Moreno, F | [[Category: Moreno, F B.M B.]] | ||
[[Category: Rocha, B | [[Category: Rocha, B A.M.]] | ||
[[Category: Santi-Gadelha, T.]] | [[Category: Santi-Gadelha, T.]] | ||
[[Category: Souza, E | [[Category: Souza, E P.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: MN]] | [[Category: MN]] | ||
| Line 29: | Line 29: | ||
[[Category: x-ray diffraction]] | [[Category: x-ray diffraction]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:53:14 2008'' | ||
Revision as of 17:53, 21 February 2008
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Native Crystal Structure of NO releasing inductive lectin from seeds of the Canavalia maritima (ConM)
OverviewOverview
Here, we report the crystallographic study of a lectin from Canavalia maritima seeds (ConM) and its relaxant activity on vascular smooth muscle, to provide new insights into the understanding of structure/function relationships of this class of proteins. ConM was crystallized and its structure determined by standard molecular replacement techniques. The amino acid residues, previously suggested incorrectly by manual sequencing, have now been determined as I17, I53, S129, S134, G144, S164, P165, S187, V190, S169, T196, and S202. Analysis of the structure indicated a dimer in the asymmetric unit, two metal binding sites per monomer, and loops involved in the molecular oligomerization. These confer 98% similarity between ConM and other previously described lectins, derived from Canavalia ensiformis and Canavalia brasiliensis. Our functional data indicate that ConM exerts a concentration-dependent relaxant action on isolated aortic rings that probably occurs via an interaction with a specific lectin-binding site on the endothelium, resulting in a release of nitric oxide.
About this StructureAbout this Structure
2CWM is a Protein complex structure of sequences from Canavalia maritima with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Native crystal structure of a nitric oxide-releasing lectin from the seeds of Canavalia maritima., Gadelha CA, Moreno FB, Santi-Gadelha T, Cajazeiras JB, Rocha BA, Assreuy AM, Lima Mota MR, Pinto NV, Passos Meireles AV, Borges JC, Freitas BT, Canduri F, Souza EP, Delatorre P, Criddle DN, de Azevedo WF Jr, Cavada BS, J Struct Biol. 2005 Dec;152(3):185-94. Epub 2005 Nov 14. PMID:16337811
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