Coupling of folding and binding in the PTB domain of the signaling protein Shc

Amjad Farooq, Lei Zeng, Kelley S. Yan, Kodi S. Ravichandran, Ming Ming Zhou

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

The notion that certain proteins lack intrinsic globular structure under physiological conditions and that the attainment of fully folded structure only occurs upon the binding of target molecules has been recently gaining popularity. We report here the solution structure of the PTB domain of the signaling protein Shc in the free form. Comparison of this structure with that of the complex form, obtained previously with a phosphopeptide ligand, reveals that the Shc PTB domain is structurally disordered in the free form, particularly around the regions constituting the peptide binding pocket. The binding of the ligand appears to reorganize this pocket through local folding events triggering a conformational switch between the free and the complex forms.

Original languageEnglish
Pages (from-to)905-913
Number of pages9
JournalStructure
Volume11
Issue number8
DOIs
StatePublished - Aug 1 2003
Externally publishedYes

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Ligands
Phosphopeptides
Peptides
Proteins
Protein Domains

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

Cite this

Coupling of folding and binding in the PTB domain of the signaling protein Shc. / Farooq, Amjad; Zeng, Lei; Yan, Kelley S.; Ravichandran, Kodi S.; Zhou, Ming Ming.

In: Structure, Vol. 11, No. 8, 01.08.2003, p. 905-913.

Research output: Contribution to journalArticle

Farooq, Amjad ; Zeng, Lei ; Yan, Kelley S. ; Ravichandran, Kodi S. ; Zhou, Ming Ming. / Coupling of folding and binding in the PTB domain of the signaling protein Shc. In: Structure. 2003 ; Vol. 11, No. 8. pp. 905-913.
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