1oy2 | pdb_00001oy2
From Proteopedia
Coupling of Folding and Binding in the PTB Domain of the Signaling Protein Shc
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Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Coupling of folding and binding in the PTB domain of the signaling protein Shc.,Farooq A, Zeng L, Yan KS, Ravichandran KS, Zhou MM Structure. 2003 Aug;11(8):905-13. PMID:12906822[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. ReferencesContents | ||||||||||||||||||||
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