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  • 1
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray studies of snake gourd lectin: homology with type II ribosome-inactivating proteins (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 912-914 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The lectin from the seeds of snake gourd (Trichosanthes anguina) has been crystallized in two forms using the hanging-drop method. Both the forms are hexagonal, with the asymmetric unit containing one subunit consisting of two polypeptide chains linked through disulfide bridges. Intensity data from one of the forms were collected at room temperature as well as at low temperature to 3 Å resolution. Molecular-replacement studies indicate that the lectin is homologous to type II ribosome-inactivating proteins. Partial refinement confirms this conclusion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901004620
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  • 2
    Electronic Resource
    Electronic Resource
    Homology between jacalin and artocarpin from jackfruit (Artocarpus integrifolia) seeds. Partial sequence and preliminary crystallographic studies of artocarpin (1997)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 53 (1997), S. 469-471 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Jacalin and artocarpin, the two lectins from jackfruit (Artocarpus integrifolia) seeds, have different physicochemical properties and carbohydrate-binding specificities. However, comparison of the partial amino-acid sequence of artocarpin with the known sequence of jacalin indicates close to 50% sequence identity. Artocarpin crystallizes in two forms, both monoclinic P21, with one and two tetramic molecules, respectively, in the asymmetric units of form I (a = 69.9, b = 73.7, c = 60.6 Å and β = 95.1°) and form II (a = 87.6, b = 72.2, c = 92.6 Å and β = 101.1°). Both the crystal structures have been solved by the molecular replacement method using the known structure of jacalin as the search model and one of them partially refined, confirming that the two lectins are indeed homologous.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444997000851
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  • 3
    Electronic Resource
    Electronic Resource
    The combination of molecular dynamics with crystallography for elucidating protein–ligand interactions: a case study involving peanut lectin complexes with T-antigen and lactose (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1584-1594 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Peanut lectin binds T-antigen [Galβ(1–3)GalNAc] with an order of magnitude higher affinity than it binds the disaccharide lactose. The crystal structures of the two complexes indicate that the higher affinity for T-antigen is generated by two water bridges involving the acetamido group. Fresh calorimetric measurements on the two complexes have been carried out in the temperature range 280–313 K. Four sets of nanosecond molecular-dynamics (MD) simulations, two at 293 K and the other two at 313 K, were performed on each of the two complexes. At each temperature, two somewhat different protocols were used to hydrate the complex in the two runs. Two MD runs under slightly different conditions for each complex served to assess the reliability of the approach for exploring protein–ligand interactions. Enthalpies based on static calculations and on MD simulations favour complexation involving T-antigen. The simulations also brought to light ensembles of direct and water-mediated protein–sugar interactions in both the cases. These ensembles provide a qualitative explanation for the temperature dependence of the thermodynamic parameters of peanut lectin–T-antigen interaction and for the results of one of the two mutational studies on the lectin. They also support the earlier conclusion that the increased affinity of peanut lectin for T-antigen compared with that for lactose is primarily caused by additional water bridges involving the acetamido group. The calculations provide a rationale for the observed sugar-binding affinity of one of the two available mutants. Detailed examination of the calculations point to the need for exercising caution in interpreting results of MD simulations: while long simulations are not possible owing to computational reasons, it is desirable to carry out several short simulations with somewhat different initial conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901011957
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  • 4
    Electronic Resource
    Electronic Resource
    X-ray studies on crystalline complexes involving amino acids and peptides. XXXV. Invariance and variability in amino acid aggregation in the complexes of maleic acid with L-histidine and L-lysine (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 690-696 
    Details
    ISSN: 1600-5740
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The crystal structures of complexes of maleic acid with L-histidine and L-lysine have been determined. The two crystallographically independent amino acid molecules in the L-histidine complex have different closed conformations, while the lysine molecule in its complex has the most favourable conformation sterically with an all-trans sidechain trans to the α-carboxylate group. The maleic acid molecules exist as semi-maleate ions of similar conformation and contain a symmetric O...H...O hydrogen bond. Amino acid cations and semi-maleate anions aggregate into alternate layers in both the structures. The arrangement of molecules in the histidine layer in L-histidine semi-maleate is closer to that in the crystals of the free amino acid than in other L-histidine complexes. On the other hand, the arrangement of lysine molecules in its semi-maleate complex is different from any observed so far. However, the well established characteristic interaction patterns involving amino and carboxylate groups still play a major role in holding the molecules together in the crystal of the complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0108768100002202
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    Paper (German National Licenses)
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