Articles written in Journal of Biosciences
Volume 36 Issue 3 August 2011 pp 461-469 Articles
The special AT-rich DNA-binding protein 1 (SATB1) is a matrix attachment region (MAR)-binding protein that acts as a global repressor via recruitment of CtBP1:HDAC1-containing co-repressors to its binding targets. The N-terminal PSD95/Dlg-A/ZO-1 (PDZ)-like domain of SATB1 mediates interactions with several chromatin proteins. In the present study, we set out to address whether the PDZ-domain-mediated interactions of SATB1 are critical for its
Volume 40 Issue 5 December 2015 pp 891-907 Articles
The Asian elephant
Volume 43 Issue 1 March 2018 pp 155-171 Review
Protein scaffolds as essential backbones for organization of supramolecular signalling complexes are a recurrent theme inseveral model systems. Scaffold proteins preferentially employ linear peptide binding motifs for recruiting their interactionpartners. PDZ domains are one of the more commonly encountered peptide binding domains in several proteins includingthose involved in scaffolding functions. This domain is known for its promiscuity both in terms of ligand selection, mode ofinteraction with its ligands as well as its association with other protein interaction domains. PDZ domains are subject toseveral means of regulations by virtue of their functional diversity. Additionally, the PDZ domains are refractive to theeffect of mutations and maintain their three-dimensional architecture under extreme mutational load. The biochemical andbiophysical basis for this selectivity as well as promiscuity has been investigated and reviewed extensively. The presentreview focuses on the plasticity inherent in PDZ domains and its implications for modular organization as well as evolutionof cellular signalling pathways in higher eukaryotes.