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The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex
The structure of the GroEL–GroES–(ADP)7 complex reveals how large en bloc movements of the cis ring's intermediate and apical domains enable bound GroES to stabilize a folding chamber with ADP confined to the cisRing, suggesting a model for an ATP-driven folding cycle that requires a double toroid.
Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA
Two crystal structures of the glucocorticoid receptor DNA-binding domain complexed with DNA are reported. The domain has a globular fold which contains two Zn-nucleated substructures of distinct
The 2.0 Å crystal structure of a heterotrimeric G protein
The structure of a heterotrimeric G protein reveals the mechanism of the nucleotide-dependent engagement of the α and βγ subunits that regulates their interaction with receptor and effector
Crystal structure of a yeast TBP/TATA-box complex
The 2.5 Å crystal structure of a TATA-box complex with yeast TBP shows that the eight base pairs of the TATA box bind to the concave surface of TBP by bending towards the major groove with
The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally symmetrical rings stacked back-to-back with dyad symmetry. The subunits
Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain.
Stereo-specific high-affinity binding by an isolated PH domain is demonstrated and further support a functional role for PH domains in the regulation of PLC isoforms and a possible general role forPH domains in membrane association is suggested.
Structural determinants of nuclear receptor assembly on DNA direct repeats
The stereochemistry suggests a mechanism by which heterodimers recognize the inter-half-site spacing between direct repeats of the consensus sequence 5′-AGGTCA-3′ separated by one to five base pairs.