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PDBsum entry 3ax4
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Sugar binding protein
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PDB id
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3ax4
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PDB id:
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| Name: |
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Sugar binding protein
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Title:
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Three-dimensional structure of lectin from dioclea violacea and comparative vasorelaxant effects with dioclea rostrata
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Structure:
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Lectin. Chain: a
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Source:
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Dioclea violacea. Organism_taxid: 192415. Other_details: seeds
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Resolution:
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2.61Å
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R-factor:
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0.230
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R-free:
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0.274
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Authors:
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M.J.B.Bezerra,G.A.Bezerra,J.L.Martins,K.S.Nascimento,C.S.Nagano, K.Gruber,A.M.Assereuy,P.Delatorre,B.A.M.Rocha,B.S.Cavada
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Key ref:
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M.J.Bezerra
et al.
(2013).
Crystal structure of Dioclea violacea lectin and a comparative study of vasorelaxant properties with Dioclea rostrata lectin.
Int J Biochem Cell Biol,
45,
807-815.
PubMed id:
DOI:
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Date:
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29-Mar-11
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Release date:
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04-Apr-12
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PROCHECK
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Headers
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References
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I1SB09
(I1SB09_DIOVO) -
Lectin from Dioclea violacea
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Seq:
Struc:
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237 a.a.
232 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Int J Biochem Cell Biol
45:807-815
(2013)
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PubMed id:
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Crystal structure of Dioclea violacea lectin and a comparative study of vasorelaxant properties with Dioclea rostrata lectin.
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M.J.Bezerra,
N.V.Rodrigues,
A.d.e. .F.Pires,
G.A.Bezerra,
C.B.Nobre,
K.L.Alencar,
P.M.Soares,
K.S.do Nascimento,
C.S.Nagano,
J.L.Martins,
K.Gruber,
A.H.Sampaio,
P.Delatorre,
B.A.Rocha,
A.M.Assreuy,
B.S.Cavada.
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ABSTRACT
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Lectins from Diocleinae subtribe belong to the family of legume lectins and are
characterized by high identity between their amino acids sequences. It has been
shown that punctual differences in amino acid sequences, such as one single
amino acid or an alternative conformation, represent changes in biological
activities caused by these lectins. Therefore, a more detailed understanding of
three-dimensional structures of these proteins is essential for accurate
analyzing the relationship between structure and function. In this study lectins
purified from the seeds of Dioclea violacea (DVL) and Dioclea rostrata (DRL)
were compared with regard to crystal structure and vasorelaxant properties.
Differences in structure of lectins were found to be reflected in differences in
vasorelaxant effects based on their high specificity and selectivity for cell
glycans. Binding activity was related to the position of specific residues in
the carbohydrate recognition domain (CRD). DVL complexed structure was solved by
X-ray crystallography and was compared to native DVL and DRL. Therefore, DVL was
co-crystallized with X-Man, and a molecular modeling with X-Man complexed with
DVL was done to compare the complexed and native forms adjusted fit. The
relatively narrow and deep CRD in DVL promotes little interaction with
carbohydrates; in contrast, the wider and shallower CRD in DRL favors
interaction. This seems to explain differences in the level of relaxation
induced by DVL (43%) and DRL (96%) in rat aortic rings.
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