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  • 1
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The process whereby the immune system generates antibodies of higher affinities during a response to antigen (affinity maturation) is a prototypical example of molecular evolution. Earlier studies have been confined to antibodies specific for small molecules (haptens) rather than for proteins. We ...
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Antigen recognition by T lymphocytes is mediated by cell-surface glycoproteins known as T-cell antigen receptors (TCRs). These are composed of α and β, or γ and δ, polypeptide chains with variable (V) and constant (C) regions. In contrast to αβ TCRs, which ...
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  • 3
    ISSN: 1545-9985
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] 'Superantigens' (SAgs) trigger the massive activation of T cells by simultaneous interactions with MHC and TCR receptors, leading to human diseases. Here we present the first crystal structure, at 2.5-Å resolution, of a complete ternary complex between a SAg and its two receptors, HLA-DR1/HA ...
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Immunological reviews 163 (1998), S. 0 
    ISSN: 1600-065X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Summary: Superantigens (SAGs) are a class of disease-causing and immunostimulatory proteins of bacterial or viral origin that activate T cells by binding to the Vβ domain of the T-cell antigen receptor (TCR), The three-dimensional structure of the complex between a TCR β chain (mouse Vβ8.2-Jβ2.l-Cβ1) and the SAG staphylococcal enterotoxin d (SEC3) has been recently determined. The complementarity-determining region 2 (CDR2) of the β chain and, to lesser extents, CDR1 and hypervariable region 4 (HV4) bind in a cleft between the small and large domains of the SAG, A model of the TCR-SAG-peptide/MHC complex constructed from available crystal structures reveals how the SAG acts as a wedge between the TCR and MHC, thereby displacing die antigen in peptide away from the TCR and circumventing the normal mechanism for T-cell activation by peptide/MHC, To evaluate the actual contribution of individual SAG residues to stabilizing the VβCβ-SEC3 complex, as well as to investigate the relationship between the affinity of SAGs for TCR and MHC and their ability to activate T cells, we measured the binding of a set of SEC3 mutants to a soluble recombinant TCR β chain and to the human MHC class II molecule HLA-DR1. We show that there is direct correlation between affinity and ability to stimulate T cells, with SAGs having the highest affinity for the TCR being die most biologically active. We also find that there is an interplay between TCR-SAG and SAG-MHC interactions in determining mitogenic potency, such that a small increase in die affinity of a SAG for MHC can overcome a large decrease in the SAG's affinity for die TCR, Finally, we observe that those SEC3 residues that make the greatest energetic contribution to stabilizing the VβCβ-SEC3 complex are strictly conserved among enterotoxins reactive with mouse Vβ8.2, thereby explaining why SAGs having other residues at diese positions show different Vβ-binding specificities.
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  • 5
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] We present the crystal structures, at 3.5 A resolution, of the bacterial SAgs SEC2 and SEC3 each bound to the extracellular portion of the p-chain (VP8.2JP2.1CP1) of a mouse TCR (designated 14.3.d) specific for a haemagglutinin peptide of influenza virus in the context of I-Ed (Table 1; Fig. 1). ...
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  • 6
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature structural biology 5 (1998), S. 412-414 
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] X-ray crystallographic studies of different types of protein–protein interfaces have revealed that these are generally characterized by a high degree of both shape and charge complementarity. This finding applies to both oligomeric proteins and to various protein–protein complexes, such ...
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  • 7
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Immunology 17 (1999), S. 435-466 
    ISSN: 0732-0582
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Notes: Abstract Superantigens (SAGs) are a class of immunostimulatory and disease-causing proteins of bacterial or viral origin with the ability to activate large fractions (5-20%) of the T cell population. Activation requires simultaneous interaction of the SAG with the Vbeta domain of the T cell receptor (TCR) and with major histocompatibility complex (MHC) class II molecules on the surface of an antigen-presenting cell. Recent advances in knowledge of the three-dimensional structure of bacterial SAGs, and of their complexes with MHC class II molecules and the TCR beta chain, provide a framework for understanding the molecular basis of T cell activation by these potent mitogens. These structures along with those of TCR-peptide/MHC complexes reveal how SAGs circumvent the normal mechanism for T cell activation by peptide/MHC and how they stimulate T cells expressing TCR beta chains from a number of different families, resulting in polyclonal T cell activation. The crystal structures also provide insights into the basis for the specificity of different SAGs for particular TCR beta chains, and for the observed influence of the TCR alpha chain on SAG reactivity. These studies open the way to the design of SAG variants with altered binding properties for TCR and MHC for use as tools in dissecting structure-activity relationships in this system.
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  • 8
    Publication Date: 2018-08-02
    Description: Sensors, Vol. 18, Pages 2503: Grey Model Optimized by Particle Swarm Optimization for Data Analysis and Application of Multi-Sensors Sensors doi: 10.3390/s18082503 Authors: Chenming Li Hongmin Gao Junlin Qiu Yao Yang Xiaoyu Qu Yongchang Wang Zhuqing Bi Data on the effective operation of new pumping station is scarce, and the unit structure is complex, as the temperature changes of different parts of the unit are coupled with multiple factors. The multivariable grey system prediction model can effectively predict the multiple parameter change of a nonlinear system model by using a small amount of data, but the value of its q parameters greatly influences the prediction accuracy of the model. Therefore, the particle swarm optimization algorithm is used to optimize the q parameters and the multi-sensor temperature data of a pumping station unit is processed. Then, the change trends of the temperature data are analyzed and predicted. Comparing the results with the unoptimized multi-variable grey model and the BP neural network prediction method trained under insufficient data conditions, it is proved that the relative error of the multi-variable grey model after optimizing the q parameters is smaller.
    Electronic ISSN: 1424-8220
    Topics: Chemistry and Pharmacology , Electrical Engineering, Measurement and Control Technology
    Published by MDPI Publishing
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