Steroid-Protein Interactions

Discovering Domains Mediating Protein Interactions

Background: Protein-protein interactions do not provide any direct information re‌garding the domains within the proteins that mediate the interactions. The majority of proteins are multi domain proteins and the interaction between them is often defined by the pairs of their domains. Most of the former studies focus only on interacting do‌main pairs. However they do not consider the in...

Functional Protein Interactions in Steroid Receptor-Chaperone Complexes

Heat shock protein 90 (Hsp90) is unique in that it chaperones a select group of client proteins and assists their folding in preparation for key regulatory roles in cellular signalling. Steroid receptors are among the most extensively studied Hsp90 chaperone substrates and belong to the large nuclear receptor superfamily of hormone-activated transcription factors that respond to hormonal cues t...

Mass Spectrometry-Based Strategies for Biomolecular Structure Analysis: Steroid Metabolites Structures and Protein-Protein Interactions

Organization of cytochrome P450 enzymes involved in sex steroid synthesis: PROTEIN-PROTEIN INTERACTIONS IN LIPID MEMBRANES.

Mounting evidence underscores the importance of protein-protein interactions in the functional regulation of drug-metabolizing P450s, but few studies have been conducted in membrane environments, and none have examined P450s catalyzing sex steroid synthesis. Here we report specific protein-protein interactions for full-length, human, wild type steroidogenic cytochrome P450 (P450, CYP) enzymes: ...

discovering domains mediating protein interactions

background: protein-protein interactions do not provide any direct information re­garding the domains within the proteins that mediate the interactions. the majority of proteins are multi domain proteins and the interaction between them is often defined by the pairs of their domains. most of the former studies focus only on interacting do­main pairs. however they do not consider the interaction...