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  • 1
    Electronic Resource
    Electronic Resource
    THE STRUCTURE OF THE T CELL ANTIGEN RECEPTOR (1996)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Immunology 14 (1996), S. 563-590 
    Details
    ISSN: 0732-0582
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Notes: Abstract Recent crystallographic studies of T cell antigen receptor (TCR) fragments from the alpha and beta chains have now confirmed the expected structural similarity to corresponding immunoglobulin domains. Although the three-dimensional structure of a complete TCR alphabeta heterodimer has not yet been determined, these results support the view that the extracellular region should resemble an immunoglobulin Fab fragment with the antigen-binding site formed from peptide loops homologous to immunoglobulin complementarity-determining regions (CDR). These preliminary results suggest that CDR1 and CDR2 may be less variable in structure than their immunoglobulin counterparts, consistent with the idea that they may interact preferentially with the less polymorphic regions of the molecules of the major histocompatibility complex. The region on the variable beta domain responsible for superantigen recognition is analyzed in detail. The implications for T cell activation from the interactions observed between domains of the alpha and beta chains are also discussed in terms of possible dimerization and allosteric mechanisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.immunol.14.1.563
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Structure of insulin in 4-zinc insulin (1976)
    [s.l.] : Nature Publishing Group
    Nature 261 (1976), S. 166-168 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The electron density map of 4-zinc pig insulin was phased on data from three isomorphous derivatives; a lead acetate derivative (3 sites) to 2.8-Å resolution; a mercuric acetate-2-hydroxybenzaldehyde derivative (3 sites) to 4.5 Å; and an iodo derivative formed by covalent attachment of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/261166a0
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Crystallization, preliminary X-ray diffraction study, and crystal packing of a complex between anti-Hen lysozyme antibody F9.13.7 and Guinea-fowl lysozyme (1993)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 15 (1993), S. 209-212 
    Details
    ISSN: 0887-3585
    Keywords: crystallization ; antilysozyme system ; epitope ; antigen-antibody complex ; cross-reactivity ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The complex formed between the Fab fragment of a murine monoclonal anti-hen egg lysozyme antibody F9.13.7 and the het-erologous antigen Guinea-fowl egg lysozyme has been crystallized by the hanging drop technique. The crystals, which diffract X-rays to 3 Å resolution, belong to the monoclinic space group P21, with a = 83.7 Å, b = 195.5 Å, c = 50.2 Å, β = 108.5° and have two molecules of the complex in the asymmetric unit The three-dimensional structure has been determined from a preliminary data set to 4 Å using molecular replacement techniques. The lysozyme-Fab complexes are arranged with their long molecular axes approximately parallel to the crystallo-graphic unique axis. Fab F9.13.7 binds an anti-genie determinant that partially overlaps the epitope recognized by antilysozyme antibody HyHEL10. © 1993 Wiley-Liss, Inc.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340150211
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    Paper (German National Licenses)
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