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Crystal structure of Streptococcus dysgalactiae-derived mitogen reveals a zinc-binding site and alterations in TcR binding.

Crystal structure of Streptococcus dysgalactiae-derived mitogen reveals a zinc-binding site and alterations in TcR binding. Research Abstract Details 

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  • Crystal structure of Streptococcus dysgalactiae-derived mitogen reveals a zinc-binding site and alterations in TcR binding. Abstract Text:

    susanna saarinenSusanna Saarinen,hidehito katoHidehito Kato,takehiko uchiyamaTakehiko Uchiyama,tohru miyoshi-akiyamaTohru Miyoshi-Akiyama,anastassios c papageorgiouAnastassios C Papageorgiou,susanna saarinenSusanna Saarinen,hidehito katoHidehito Kato,takehiko uchiyamaTakehiko Uchiyama,tohru miyoshi-akiyamaTohru Miyoshi-Akiyama,anastassios c papageorgiouAnastassios C Papageorgiou,

    Bacterial superantigens are protein toxins with an ability to cause serious diseases in humans by activating a large number of T cells. Streptococcus dysgalactiae-derived mitogen (SDM) is a novel superantigen that is distinct from other known superantigens based on phylogenetic analysis. The X-ray structure of SDM has been determined at 1.95 A resolution. SDM shares the same characteristic fold with other superantigens, but it shows a major structural difference due to the lack of the alpha5 helix between the beta10 and beta11 strands. A bound zinc ion was identified in the structure at the C-terminal domain of the molecule. SDM appears to bind to the major histocompatibility complex class II beta-chain through the zinc-binding site, as described by mutagenesis data and structural comparisons. T-cell binding instead shows a significant difference compared to other superantigens. The mutation of Asn11 (a conserved residue that is known to be significant for T-cell-receptor binding in other superantigens) and Lys15 to Ala did not cause any decrease in the mitogenic activity of SDM. This observation and the lack of the alpha5 helix suggest alterations in T-cell-receptor binding.

    Crystal structure of Streptococcus dysgalactiae-derived mitogen reveals a zinc-binding site and alterations in TcR binding. Publishing Authors By Initials

    s saarinenS Saarinen,h katoH Kato,t uchiyamaT Uchiyama,t miyoshi-akiyamaT Miyoshi-Akiyama,ac papageorgiouAC Papageorgiou,s saarinenS Saarinen,h katoH Kato,t uchiyamaT Uchiyama,t miyoshi-akiyamaT Miyoshi-Akiyama,ac papageorgiouAC Papageorgiou,

    For similar abstracts research abstracts see: abstracts research

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    Crystal structure of Streptococcus dysgalactiae-derived mitogen reveals a zinc-binding site and alterations in TcR binding. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of molecular biology

    VOLUME: 373

    Page Numbers: 1089-97

    Journal Abbreviation: J. Mol. Biol.

    ISSN: 0022-2836

    DAY: 21

    MONTH: 08

    YEAR: 2007

    Crystal structure of Streptococcus dysgalactiae-derived mitogen reveals a zinc-binding site and alterations in TcR binding. Information

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    LANGUAGE: eng

    NlmUniqueID: 2985088

    Crystal structure of Streptococcus dysgalactiae-derived mitogen reveals a zinc-binding site and alterations in TcR binding. Keywords Mesh Terms:

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    Grant and Affiliation Information for Crystal structure of Streptococcus dysgalactiae-derived mitogen reveals a zinc-binding site and alterations in TcR binding.

    AFFILIATION: Turku Center for Biotechnology, University of Turku and Abo Akademi University, PO Box 123, Tykistökatu 6, BioCity, Turku 20521, Finland.

    Country: England

    England Research PublicationEngland Research Publication

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    MEDLINETA: J Mol Biol

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    ACCESSION NUMBER: 2J4X

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