2cwm
Native Crystal Structure of NO releasing inductive lectin from seeds of the Canavalia maritima (ConM)
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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 CA and MN 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
Page seeded by OCA on Wed Nov 21 09:18:36 2007