A PDZ domain recapitulates a unifying mechanism for protein folding
نویسندگان
چکیده
منابع مشابه
A PDZ domain recapitulates a unifying mechanism for protein folding.
A unifying view has been recently proposed according to which the classical diffusion-collision and nucleation-condensation models may represent two extreme manifestations of an underlying common mechanism for the folding of small globular proteins. We report here the characterization of the folding process of the PDZ domain, a protein that recapitulates the three canonical steps involved in th...
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Different models such as diffusion-collision and nucleation-condensation have been used to unravel how secondary and tertiary structures form during protein folding. However, a simple mechanism based on physical principles that provide an accurate description of kinetics and thermodynamics for such phenomena has not yet been identified. This study introduces the hypothesis that the synchronizat...
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Proteins appear to fold by diverse pathways, but variations of a simple mechanism - nucleation-condensation - describe the overall features of folding of most domains. In general, secondary structure is inherently unstable and its stability is enhanced by tertiary interactions. Consequently, an extensive interplay of secondary and tertiary interactions determines the transition-state for foldin...
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Circular permutation is a common molecular mechanism for evolution of proteins. However, such re-arrangement of secondary structure connectivity may interfere with the folding mechanism causing accumulation of folding intermediates, which in turn can lead to misfolding. We solved the crystal structure and investigated the folding pathway of a circularly permuted variant of a PDZ domain, SAP97 P...
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Using PICK1 as an example this review highlights PDZ domains support a repertoire of protein-protein interactions that regulate the subcellular localisation and function of receptors, ion channels and enzymes. PICK1 is a 416 amino acid protein that contains a PDZ domain, a coiled-coil motif/arfaptin homology domain and an acidic c-terminal. Nearly all proteins thus far reported to interact with...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2006
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0602770104