Structural analysis of a Dioclea sclerocarpa lectin: Study on the vasorelaxant properties of Dioclea lectins.
Lectins are proteins that show a variety of biological activities. However, they share in common at least one domain capable of recognizing specific carbohydrates reversibly without changing its structure. The legume lectins family is the most studied family of plant lectins, in particular the Diocleinae subtribe, which possesses high degree of structural similarity, but variable biological activities. This variability lies in small differences that can be analyzed in studies based on structures. In particular, Dioclea sclerocarpa seed lectin (DSL) presents low ability to relax endothelialized rat aorta in comparison with other Dioclea lectins such as Dioclea violacea (DVL), Dioclea virgata (DvirL) and Dioclea rostrata (DRL). The DSL relaxation mechanism relies on nitric oxide production and carbohydrate recognition domain (CRD). This feature can be explained by structural differences, since DSL has a carbohydrate recognition domain design less favorable. In addition, the presence of a glutamate residue at position 205 proved to be a decisive factor for the low relaxant effect of Dioclea lectins.
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, CE, Brazil.
Ito L
IL
Barroso-Neto
Departamento de Biologia Molecular, Universidade Federal da Paraíba, João Pessoa, PB, Brazil.
Plinio
P
Delatorre
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, CE, Brazil.
Claudener S
CS
Teixeira
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, CE, Brazil.
Jorge L A
JL
Correia
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, CE, Brazil.
João B
JB
Cajazeiras
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, CE, Brazil.
Ronniery I
RI
Pereira
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, CE, Brazil.
Kyria S
KS
Nascimento
Instituto Superior de Ciências Biomédicas, Universidade Estadual do Ceará, Fortaleza, CE, Brazil.
Eva P P
EP
Laranjeira
Instituto Superior de Ciências Biomédicas, Universidade Estadual do Ceará, Fortaleza, CE, Brazil.
Alana F
AF
Pires
Instituto Superior de Ciências Biomédicas, Universidade Estadual do Ceará, Fortaleza, CE, Brazil.
Ana M S
AM
Assreuy
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, CE, Brazil. Electronic address: bruno.rocha@ufc.br.
Bruno A M
BA
Rocha
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, CE, Brazil. Electronic address: bscavada@ufc.br.
Benildo S
BS
Cavada
D000818:Animals; D001011:Aorta / Q000187:drug effects; D001665:Binding Sites; D002241:Carbohydrates / Q000737:chemistry; D052598:Dioclea / Q000737:chemistry*; D008958:Models, Molecular; D037121:Plant Lectins / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D011485:Protein Binding; D011487:Protein Conformation; D051381:Rats; D013329:Structure-Activity Relationship; D014665:Vasodilator Agents / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*
D002241:Carbohydrates; D037121:Plant Lectins; D014665:Vasodilator Agents
Carbohydrate binding protein; Dioclea sclerocarpa; Vasorelaxant effect