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  • 1
    Electronic Resource
    Electronic Resource
    Factor B structure provides insights into activation of the central protease of the complement system (2007)
    [s.l.] : Nature Publishing Group
    Nature structural & molecular biology 14 (2007), S. 224-228 
    Details
    ISSN: 1545-9985
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Factor B is the central protease of the complement system of immune defense. Here, we present the crystal structure of human factor B at 2.3-Å resolution, which reveals how the five-domain proenzyme is kept securely inactive. The canonical activation helix of the Von Willebrand factor A (VWA) ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nsmb1210
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  • 2
    Electronic Resource
    Electronic Resource
    The structure of leech anti-platelet protein, an inhibitor of haemostasis (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1071-1078 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Leech anti-platelet protein (LAPP) from the leech Haementeria officinalis is a collagen-binding protein that inhibits the collagen-mediated adhesion of blood platelets. The crystal structure of recombinant LAPP has been determined using single isomorphous replacement with anomalous scattering combined with solvent flattening and threefold molecular averaging. The model of LAPP has been refined to 2.2 Å resolution (R factor 21.5%; free R factor 24.0%). LAPP contains an 89-residue C-terminal domain consisting of a central six-stranded antiparallel β-sheet flanked on one side by an α-helix and on the other side by two extended loops with little secondary structure. A 36-residue N-terminal region is not visible in the electron-density map. This region is rich in glycine and lacks hydrophobic residues. It probably does not have a compact globular fold, but instead has an extended conformation and is flexible. The crystal packing suggests that LAPP may form tightly interacting dimers. The fold of the C-terminal domain of LAPP closely resembles that of the N-domain of hepatocyte growth factor (HGF), which classifies LAPP as a PAN domain. However, no significant sequence homology exists between LAPP and other PAN domains. Common structural features between LAPP and the HGF N-domain include two disulfide bonds that link the α-helix to the central region of the protein and five residues with a conserved hydrophobic nature that are located in the core of the domain. These conserved structural features may be an important determinant of the PAN-domain type of fold.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901007405
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  • 3
    Electronic Resource
    Electronic Resource
    Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination (1998)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 54 (1998), S. 905-921 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A new software suite, called Crystallography & NMR System (CNS), has been developed for macromolecular structure determination by X-ray crystallography or solution nuclear magnetic resonance (NMR) spectroscopy. In contrast to existing structure-determination programs the architecture of CNS is highly flexible, allowing for extension to other structure-determination methods, such as electron microscopy and solid-state NMR spectroscopy. CNS has a hierarchical structure: a high-level hypertext markup language (HTML) user interface, task-oriented user input files, module files, a symbolic structure-determination language (CNS language), and low-level source code. Each layer is accessible to the user. The novice user may just use the HTML interface, while the more advanced user may use any of the other layers. The source code will be distributed, thus source-code modification is possible. The CNS language is sufficiently powerful and flexible that many new algorithms can be easily implemented in the CNS language without changes to the source code. The CNS language allows the user to perform operations on data structures, such as structure factors, electron-density maps, and atomic properties. The power of the CNS language has been demonstrated by the implementation of a comprehensive set of crystallographic procedures for phasing, density modification and refinement. User-friendly task-oriented input files are available for nearly all aspects of macromolecular structure determination by X-ray crystallography and solution NMR.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444998003254
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  • 4
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray analysis of Drosophila glutathione S-transferase-2 (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 725-727 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The σ-class glutathione S-transferase-2 (GST-2) from Drosophila melanogaster is predominantly found within the indirect flight muscles (IFMs), where it is bound to the `heavy' subunit of the IFM thin filament troponin complex (Tn-H). An N-terminal extension found in GST-2 is unique within the σ GST class and may be involved in its interaction with Tn-H or modulate its enzymatic function. The recombinant protein has been crystallized at room temperature using ammonium sulfate as precipitant. Synchrotron radiation was used to measure a complete native data set to 1.75 Å resolution from flash-cooled crystals. The crystals belong to one of the trigonal space groups P3121 or P3221, with unit-cell parameters a = b = 89.7, c = 131.8 Å. The self-rotation function is consistent with a GST-2 dimer in the asymmetric unit.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901003110
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  • 5
    Electronic Resource
    Electronic Resource
    Conditional optimization: a new formalism for protein structure refinement (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1820-1828 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Conditional optimization allows unlabelled loose-atom refinement to be combined with extensive application of geometrical restraints. It offers an N-particle solution for the assignment of topology to loose atoms, with weighted gradients applied to all possibilities. For a simplified test structure consisting of a polyalanine four-helical bundle, this method shows a large radius of convergence using calculated diffraction data to at least 3.5 Å resolution. It is shown that with a new multiple-model protocol to estimate σA values, this structure can be successfully optimized against 2.0 Å resolution diffraction data starting from a random atom distribution. Conditional optimization has potentials for map improvement and automated model building at low or medium resolution limits. Future experiments will have to be performed to explore the possibilities of this method for ab initio phasing of real protein diffraction data.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901015414
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  • 6
    Electronic Resource
    Electronic Resource
    Structures of complement component C3 provide insights into the function and evolution of immunity (2005)
    [s.l.] : Nature Publishing Group
    Nature 437 (2005), S. 505-511 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The mammalian complement system is a phylogenetically ancient cascade system that has a major role in innate and adaptive immunity. Activation of component C3 (1,641 residues) is central to the three complement pathways and results in inflammation and elimination of self and non-self targets. Here ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature04005
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  • 7
    Electronic Resource
    Electronic Resource
    Crystallography Crystallographic evidence for deviating C3b structure (2007)
    [s.l.] : Nature Publishing Group
    Nature 448.2007, 7154, E1-, (2 S.) 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Arising from: A. A. Ajees et al. Nature 444, 221–225 (2006); Ajees et al. reply Activation of the protein C3 into C3b in the complement pathway is a crucial step in the complement immune response against pathogenic, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature06102
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  • 8
    Electronic Resource
    Electronic Resource
    Structure of C3b reveals conformational changes that underlie complement activity (2006)
    [s.l.] : Nature Publishing Group
    Nature 444 (2006), S. 213-216 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Resistance to infection and clearance of cell debris in mammals depend on the activation of the complement system, which is an important component of innate and adaptive immunity. Central to the complement system is the activated form of C3, called C3b, which attaches covalently to target ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature05172
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  • 9
    Electronic Resource
    Electronic Resource
    C-terminal domain of transcription cofactor PC4 reveals dimeric ssDNA binding site (1997)
    [s.l.] : Nature Publishing Group
    Nature structural biology 4 (1997), S. 900-903 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Sir — In gene transcription specific activator proteins form a regulatory interface leading to recruitment of general transcription factors and activation of transcription complexes. A group of proteins termed cofactors functionally and physically mediates between activators and the basal ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nsb1197-900
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  • 10
    Electronic Resource
    Electronic Resource
    Effects of eglin-c binding to thermitase: Three-dimensional structure comparison of native thermitase and thermitase eglin-c complexes (1992)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 12 (1992), S. 63-74 
    Details
    ISSN: 0887-3585
    Keywords: subtilisin ; serine proteinase ; serine proteinase inhibitor ; induced-fit mechanism ; protein crystallography ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Thermitase is a thermostable member of the subtilisin family of serine proteases. Four independently determined crystal structures of the enzyme are compared in this study: a high resolution native one and three medium resolution complexes of thermitase with eglin-c, grown from three different calcium concentrations. It appeared that the B-factors of the thermitase eglin complex obtained at 100 mM CaCl2 and elucidated at 2.0 Å resolution are remarkably similar to those of the 1.4 Å native structure: the main chain atoms have an rms difference of only 2.3 Å2; for all atoms this difference is 4.6 Å2. The rms positional differences between these two structures of thermitase are 0.31 Å for the main chain atoms and 0.58 Å for all atoms. There results show that not only atomic positions but also temperature factors can agree well in X-ray structures determined entirely independently by procedures which differ in virtually every possible technical aspect.A detailed comparison focussed on the effects of eglin binding on the structure of thermitase. Thermitase can be considered as consisting of (1) a central core of 94 residues, plus (2) four segments of 72 residues in total which shift as rigid bodies with respect to the core, plus (3) the remaining 113 residues which show small changes but, however, cannot be described as rigid bodies. The central cores of native thermitase and the 100 mM CaCl2 thermitase:eglin complex have an rms deviation of 0.13 Å for 376 main chain atoms. One of the segments, formed by loops of the strong calcium binding site, shows differences up to 1.0 Å in Cα positions. These are probably due to crystal packing effects.The three other segments, comprising 51 residues, are affected conformational changes upon eglin binding so that the P1 to P3 binding pockets of thermitase broaden by 0.4 to 0.7 Å. The residues involved in these changes correspond with residues which change position upon inhibitor binding in other subtilisins. This suggests that an induced fit mechanism is operational during substrate recognition by subtilisins.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340120108
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