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The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex
Chaperonins assist protein folding with the consumption of ATP. They exist as multi-subunit protein assemblies comprising rings of subunits stacked back to back. In Escherichia coli, asymmetricExpand
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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 distinctExpand
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The Structure of ClpB A Molecular Chaperone that Rescues Proteins from an Aggregated State
Molecular chaperones assist protein folding by facilitating their "forward" folding and preventing aggregation. However, once aggregates have formed, these chaperones cannot facilitate proteinExpand
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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 effectorExpand
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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 withExpand
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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 subunitsExpand
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Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain.
Pleckstrin homology (PH) domains are found in many signaling molecules and are thought to be involved in specific intermolecular interactions. Their binding to several proteins and to membranesExpand
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Structural determinants of nuclear receptor assembly on DNA direct repeats
Nuclear receptor heterodimers recognize response elements composed of two direct repeats of the consensus sequence 5′-AGGTCA-3′ separated by one to five base pairs. The 1.9 Å crystal structure of theExpand
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Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
The X-ray crystal structure of the high affinity complex between the pleckstrin homology (PH) domain from rat phospholipase C-delta 1 (PLC-delta 1) and inositol-(1,4,5)-trisphosphate (Ins(1,4,5)P3)Expand
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