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- Title
Mass Spectrometry and X-ray Diffraction Analysis of Two Crystal Types of Dioclea virgata Lectin: An Antinociceptive Protein Candidate to Structure/Function Analysis.
- Authors
Delatorre, Plínio; Rocha, Bruno A. M.; Simões, Rafael C.; Pereira-Júnior, Francisco N.; Silva, Helton C.; Bezerra, Eduardo Henrique S.; Bezerra, Maria Julia B.; Marinho, Emmanuel S.; Gadelha, Carlos A. A.; Santi-Gadelha, Tatiane; Farias, Daniel L.; Assreuy, Ana Maria S.; Marques-Domingos, Gabriela F. O.; Nagano, Celso S.; Cavada, Benildo S.
- Abstract
The lectin from seeds of Dioclea virgata (DvirL) was purified in a single step affinity chromatography, sequenced by tandem mass spectrometry and submitted to crystallization and biological experiments. DvirL has a molecular mass of 25,412 ± 2 Da and the chains β and γ has 12,817 Da ± 2 and 12,612 Da ± 2, respectively. Primary sequence determination was assigned by tandem mass spectrometry and revealed a protein with 237 amino acids and 87% of identify with ConA. The protein crystals were obtained native and complexed with X-Man using vapor-diffusion method at a constant temperature of 293 K. A complete X-ray dataset was collected at 1.8 Å resolution. DvirL crystals were found to be orthorhombic, belonging to the space group I222, with a unit cell parameters a = 647.5 Å, b = 86.6 Å, c = 90.2 Å. Molecular replacement search found a solution with a correlation coefficient of 77.1% and an R of 44.6%. The present study also demonstrated that D. virgata lectin presents edematogenic and antinociceptive activities in rodents electing this protein as a candidate to structure/function analysis.
- Subjects
MASS spectrometry; LECTINS; AMINO acids; X-ray diffraction; CRYSTALLIZATION
- Publication
Applied Biochemistry & Biotechnology, 2011, Vol 164, Issue 6, p741
- ISSN
0273-2289
- Publication type
Article
- DOI
10.1007/s12010-011-9170-x