A Systematic Family-wide Investigation Reveals that ∼30% of Mammalian PDZ Domains Engage in PDZ-PDZ Interactions

作者: Bryan H Chang , Taranjit S Gujral , Ethan S Karp , Raghida BuKhalid , Viara P Grantcharova

DOI: 10.1016/J.CHEMBIOL.2011.06.013

关键词:

摘要: Summary PDZ domains are independently folded modules that typically mediate protein-protein interactions by binding to the C termini of their target proteins. However, in a few instances, have been reported dimerize with other domains. To investigate this noncanonical-binding mode further, we used protein microarrays comprising virtually every mouse domain systematically query all possible PDZ-PDZ pairs. We then fluorescence polarization retest and quantify coaffinity purification test biophysically validated context full-length Overall, discovered 37 involving 46 (∼30% tested), revealing that dimerization is more frequently than was previously appreciated. This suggests many evolved form multiprotein complexes simultaneously interacting one ligand.

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