Native crystal structure of a nitric oxide-releasing lectin from the seeds of Canavalia maritima

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 deter...

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Bibliographic Details
Published in:Journal of structural biology 2005-12, Vol.152 (3), p.185-194
Main Authors: Gadelha, Carlos Alberto de Almeida, Moreno, Frederico Bruno Mendes Batista, Santi-Gadelha, Tatiane, Cajazeiras, João Batista, Rocha, Bruno Anderson Matias da, Assreuy, Ana Maria Sampaio, Lima Mota, Mário Rogério, Pinto, Nilson Vieira, Passos Meireles, Ana Vaneska, Borges, Júlio César, Freitas, Beatriz Tupinamba, Canduri, Fernanda, Souza, Emmanuel Prata, Delatorre, Plínio, Criddle, David Neil, de Azevedo, Walter Filgueira, Cavada, Benildo Sousa
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Aorta, Thoracic - drug effects
Aorta, Thoracic - physiology
Binding Sites
Canavalia - chemistry
Canavalia - genetics
Canavalia maritima
Concanavalin A - genetics
Concanavalin A - pharmacology
Crystal structure
Crystallography, X-Ray
Endothelium, Vascular - physiology
Enzyme Inhibitors - pharmacology
In Vitro Techniques
Legume lectin
Male
Models, Molecular
Molecular Sequence Data
NG-Nitroarginine Methyl Ester - pharmacology
Nitric oxide
Nitric Oxide - metabolism
Nitric Oxide Synthase - antagonists & inhibitors
Nitric Oxide Synthase - metabolism
Phenylephrine - pharmacology
Plant Lectins - chemistry
Plant Lectins - genetics
Plant Lectins - pharmacology
Protein Conformation
Protein Structure, Quaternary
Rats
Rats, Wistar
Seeds - chemistry
Sequence Homology, Amino Acid
Static Electricity
Vascular
Vasodilation - drug effects
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Summary: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.
ISSN:1047-8477
1095-8657
DOI:10.1016/j.jsb.2005.07.012