A reinterpretation of the dimerization interface of the N‐terminal Domains of STATs
書誌事項
- 公開日
- 2003-02
- 権利情報
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- http://onlinelibrary.wiley.com/termsAndConditions#vor
- DOI
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- 10.1110/ps.0218903
- 公開者
- Wiley
この論文をさがす
説明
<jats:title>Abstract</jats:title><jats:p>The crystal structures of the N‐terminal domain (N‐domain) and the core region of the STAT family of transcription factors have been determined previously. STATs can form cooperative higher order structures (tetramers or higher oligomers) while bound to DNA. The crystal packing in the STAT4 N‐domain crystal structure, determined at 1.5 Å resolution, suggests two alternate organizations of the N‐domain dimer. We now present the results of site directed mutagenesis of residues predicted to be involved at each dimer interface. Our results indicate that the dimer interface suggested earlier as being physiologically relevant is, in fact, unlikely to be so. Given the alternative model for the N‐domain dimer, the ability of the N‐domain to mediate interactions of two STAT dimers on DNA remains unchanged.</jats:p>
収録刊行物
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- Protein Science
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Protein Science 12 (2), 361-365, 2003-02
Wiley
