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Research Article

Crystal Structures of the ATPase Domains of Four Human Hsp70 Isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78

  • Magdalena Wisniewska,

    Affiliation: Structural Genomics Consortium, Karolinska Institutet, Stockholm, Sweden

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  • Tobias Karlberg,

    Affiliation: Structural Genomics Consortium, Karolinska Institutet, Stockholm, Sweden

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  • Lari Lehtiö,

    Affiliation: Structural Genomics Consortium, Karolinska Institutet, Stockholm, Sweden

    Current address: Department of Biochemistry and Pharmacy, Åbo Akademi, Turku, Finland

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  • Ida Johansson,

    Affiliation: Structural Genomics Consortium, Karolinska Institutet, Stockholm, Sweden

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  • Tetyana Kotenyova,

    Affiliation: Structural Genomics Consortium, Karolinska Institutet, Stockholm, Sweden

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  • Martin Moche,

    Affiliation: Structural Genomics Consortium, Karolinska Institutet, Stockholm, Sweden

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  • Herwig Schüler mail

    herwig.schuler@ki.se

    Affiliation: Structural Genomics Consortium, Karolinska Institutet, Stockholm, Sweden

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  • Published: January 11, 2010
  • DOI: 10.1371/journal.pone.0008625
  • Published in PLOS ONE

Reader Comments (1)

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Good work

Posted by naveenis4u on 28 Jan 2011 at 08:37 GMT

The compressive view of 5 different Hsp70 family proteins in co-ordination with ADP and metal ion is interesting. In addition the conservenes of Hsp70 and its family proteins were further corroborated by explain the isomorphic specificity of nucleotide binding. However, it’s over all regulation with partner proteins and substrate has to be addressed further.

No competing interests declared.