Small-angle X-ray scattering (SAXS) in combination with NMR has also been used to determine the structure of PDZ-containing proteins. This review focuses on the advances made in the fields of structural biology, proteomic applications, and regulatory mechanisms of PDZ-mediated interactions.Īt present, more than 200 structures of PDZ domains - either the PDZ domains alone, their complexes with binding partners, or PDZ-PDZ dimers - have been determined by NMR and X-ray crystallography. PDZ-containing proteins interact with many proteins within cells, so studying the regulatory mechanisms of PDZ protein-protein interactions, such as phosphorylation, autoinhibition, and allostery, is also vital to understand their biology. Proteomic methods, such as large scale protein arrays and peptide libraries, have also been used to understand the binding properties of PDZ protein-protein interactions at a genome-wide level, which may provide clues about novel functions of proteins of interest in various cells.
Structural analysis of PDZ domains and PDZ-mediated interactions by NMR and X-ray crystallographic methods in conjunction with computational methods has provided insights into the specificity or promiscuity of PDZ protein-protein interactions. PDZ domains typically recognize the extreme C-termini of target proteins, but some also recognize the internal sequence motif of target proteins through a single binding site on the domains. PDZ domains are small and often modular entities consisting of 5 or 6 β-stranded and 2 or 3 α-helical structures.
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