Unknown

Dataset Information

0

Production of unstable proteins through the formation of stable core complexes.


ABSTRACT: Purification of proteins that participate in large transient complexes is impeded by low amounts, heterogeneity, instability and poor solubility. To circumvent these difficulties we set up a methodology that enables the production of stable complexes for structural and functional studies. This procedure is benchmarked and applied to two challenging protein families: the human steroid nuclear receptors (SNR) and the HIV-1 pre-integration complex. In the context of transcriptional regulation studies, we produce and characterize the ligand-binding domains of the glucocorticoid nuclear receptor and the oestrogen receptor beta in complex with a TIF2 (transcriptional intermediary factor 2) domain containing the three SNR-binding motifs. In the context of retroviral integration, we demonstrate the stabilization of the HIV-1 integrase by formation of complexes with partner proteins and DNA. This procedure provides a powerful research tool for structural and functional studies of proteins participating in non-covalent macromolecular complexes.

SUBMITTER: Levy N 

PROVIDER: S-EPMC4800440 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC8390856 | biostudies-literature
| S-EPMC2043554 | biostudies-literature
| S-EPMC6768856 | biostudies-literature
| S-EPMC5579112 | biostudies-literature
| S-EPMC5127780 | biostudies-literature
| S-EPMC4290805 | biostudies-literature
| S-EPMC6805852 | biostudies-literature
| S-EPMC7392606 | biostudies-literature
| S-EPMC3730348 | biostudies-literature
| S-EPMC23037 | biostudies-literature