Research Topics
Genomes and Genes
Species
| P B SiglerSummaryAffiliation: Yale University Country: USA Publications
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Publications
Structure and function in GroEL-mediated protein foldingP B Sigler
Department of Molecular Biophysics and Biochemistry, School of Medicine, Yale University, New Haven, Connecticut 06510, USA
Annu Rev Biochem 67:581-608. 1998..This process allows the polypeptide to achieve its final native state, if folding was completed, or to recycle to another chaperonin molecule, if the folding process did not result in a form committed to the native state...
The 2.1-A crystal structure of an archaeal preinitiation complex: TATA-box-binding protein/transcription factor (II)B core/TATA-boxP F Kosa
Department of Molecular Biophysics and Biochemistry, and the Howard Hughes Medical Institute, Yale University, 260 Whitney Avenue, JWG 423, New Haven CT 06511, USA
Proc Natl Acad Sci U S A 94:6042-7. 1997....- Distinct actions of cis and trans ATP within the double ring of the chaperonin GroELH S Rye
Howard Hughes Medical Institute, Department of Genetics, School of Medicine, Yale University, New Haven, Connecticut 06510, USA
Nature 388:792-8. 1997..These observations offer an explanation of why GroEL functions as a double-ring complex... - The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complexZ Xu
The Howard Hughes Medical Institute, The Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510, USA
Nature 388:741-50. 1997..When combined with new functional results, this negative allosteric mechanism suggests a model for an ATP-driven folding cycle that requires a double toroid... - The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma SJ P Noel
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510
Nature 366:654-63. 1993.... - Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane TranslocationM Han
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA
Structure 9:869-80. 2001..They compete with G proteins for binding to activated phosphorylated receptors, initiate receptor internalization, and activate additional signaling pathways... - Crystal structure of the yeast TFIIA/TBP/DNA complexJ H Geiger
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06510, USA
Science 272:830-6. 1996..The four-helix-bundle domain projects away from the TBP/TATA complex, thereby presenting a substantial surface for further protein-protein interactions... - Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilusY Wang
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511, USA
Nat Struct Biol 4:650-6. 1997..The exchange mechanism may have useful implications for receptor-induced exchange in heterotrimeric G proteins... - The crystal structure of a hyperthermophilic archaeal TATA-box binding proteinB S DeDecker
Department of Molecular Biophysics and Biochemistry and the Howard Hughes Medical Institute, Yale University, New Haven, CT 06511 8114, USA
J Mol Biol 264:1072-84. 1996..The total reliance on a hydrophobic interface with DNA may explain the enhanced affinity of PwTBP for its DNA promoter at higher temperatures and increased salt concentration... - Structural determinants for activation of the alpha-subunit of a heterotrimeric G proteinD G Lambright
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510
Nature 369:621-8. 1994..The changes are distinct from those observed in other members of the GTPase superfamily... - The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma SD C Boisvert
Department of Genetics, Yale University School of Medicine, New Haven, Connecticut 06510, USA
Nat Struct Biol 3:170-7. 1996..Although bound ATP induces modest conformational shifts in the equatorial domain, the stereochemistry that functionally coordinates GroEL's affinity for nucleotides, polypeptide, and GroES remains uncertain... - DNA-binding mechanism of the monomeric orphan nuclear receptor NGFI-BG Meinke
Department of Molecular Biophysics and Biochemistry and the Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06511, USA
Nat Struct Biol 6:471-7. 1999.... - The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversityL Chen
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511, USA
Cell 99:757-68. 1999..Our structural analysis, combined with other results, suggests that various modes of molecular plasticity are responsible for tight promiscuous binding of nonnative substrates and their release into the shielded cis assembly... - The structural basis for the oriented assembly of a TBP/TFB/promoter complexO Littlefield
Department of Molecular Biophysics, Yale University, New Haven CT 06511, USA
Proc Natl Acad Sci U S A 96:13668-73. 1999..This interaction is important in determining the level of basal transcription and explicitly defines the direction of transcription... - Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domainK M Ferguson
Department of Chemistry, Yale University, New Haven, Connecticut 06510, USA
Cell 83:1037-46. 1995..Using electrostatics and varying levels of head-group specificity, PH domains may localize and orient signaling proteins, providing a general membrane targeting and regulatory function... - Crystal structure of a yeast TBP/TATA-box complexY Kim
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510
Nature 365:512-20. 1993..The severe bend and a positive writhe radically alter the trajectory of the flanking B-form DNA... - Atomic structure of progesterone complexed with its receptorS P Williams
Department of Molecular Biophysics and Biochemistry, and the Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06510, USA
Nature 393:392-6. 1998..The structure also indicates that the analogous 3-keto-steroid receptors may have a similar mechanism of action... - Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 AK C Slep
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511, USA
Nature 409:1071-7. 2001..Effector binding to a nucleotide-dependent site on alpha(t) sequesters PDEgamma residues implicated in PDE inhibition, and potentiates recruitment of RGS9 for hydrolytic transition state stabilization and concomitant signal termination... - Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coliG D Van Duyne
Department of Molecular Biochemistry and Biophysics, Howard Hughes Medical Institute, Yale University, New Haven, CT 06510 USA
J Mol Biol 256:377-91. 1996.... - Sst2 is a GTPase-activating protein for Gpa1: purification and characterization of a cognate RGS-Galpha protein pair in yeastD M Apanovitch
Department of Pharmacology and Molecular Cardiobiology Program, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, Connecticut 06536, USA
Biochemistry 37:4815-22. 1998..These experiments represent the first biochemical characterization of Gpa1 and Sst2, and provide a molecular basis for their well-established biological roles in signaling and desensitization... - Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogueD L Scott
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511
Science 250:1563-6. 1990..Comparison of the bee-venom enzyme with other phospholipase structures provides compelling evidence for a common catalytic mechanism... - Crystal structure of a G-protein beta gamma dimer at 2.1A resolutionJ Sondek
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510, USA
Nature 379:369-74. 1996..The structure details interactions between G protein beta- and gamma-subunits and highlights regions implicated in effector modulation for the conserved family of G protein beta gamma dimers... - A molecular mechanism for the phosphorylation-dependent regulation of heterotrimeric G proteins by phosducinR Gaudet
Department of Molecular Biophysics, Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06511, USA
Mol Cell 3:649-60. 1999..This transition disrupts phosducin's interface with Gt beta gamma, leading to the release of unencumbered Gt beta gamma, which reassociates with the membrane and Gt alpha to form a signaling-competent Gt alpha beta gamma heterotrimer... - Structural determinants of nuclear receptor assembly on DNA direct repeatsF Rastinejad
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510, USA
Nature 375:203-11. 1995..The stereochemistry suggests a mechanism by which heterodimers recognize the inter-half-site spacing between direct repeats... - Structural basis of preinitiation complex assembly on human pol II promotersF T Tsai
Department of Molecular Biophysics and Biochemistry and the Howard Hughes Medical Institute, Yale University, New Haven, CT 06511, USA
EMBO J 19:25-36. 2000..Binding of TFIIBc is, therefore, synergistic with TBPc requiring the distortion of the TATA-box. Thus, the newly described TFIIBc-DNA interface is likely to be a key determinant for the unidirectional assembly of a functional PIC... - Activating mineralocorticoid receptor mutation in hypertension exacerbated by pregnancyD S Geller
Howard Hughes Medical Institute, Department of Genetics, Yale University School of Medicine, Boyer Center for Molecular Medicine, Room 154, 295 Congress Avenue, New Haven, CT 06510, USA
Science 289:119-23. 2000..This helix 5-helix 3 interaction is highly conserved among diverse nuclear hormone receptors, suggesting its general role in receptor activation... - Structure and importance of the dimerization domain in elongation factor Ts from Thermus thermophilusY Jiang
Department of Chemistry, Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06520, USA
Biochemistry 35:10269-78. 1996..Surprisingly, EF-Ts monomers created in this manner failed to catalyze nucleotide exchange in EF-Tu, indicating that, in vitro. T. thermophilus EF-Ts functions only as a homodimer... - The crystal structure of the bacterial chaperonin GroEL at 2.8 AK Braig
Department of Genetics, Yale University School of Medicine, Boyer Center, New Haven, Connecticut 06510
Nature 371:578-86. 1994..The three-dimensional structure places most of the mutationally defined functional sites on the channel walls and its outward invaginations, and at the ends of the cylinder... - Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domainsD M Tanenbaum
Department of Molecular Biophysics and Biochemistry and the Howard Hughes Medical Institute, Yale University, 260 Whitney Avenue, JWG 423, New Haven, CT 06511, USA
Proc Natl Acad Sci U S A 95:5998-6003. 1998..A peculiar crystal packing event displaces helix 12 in the hERalphaLBD reported here, suggesting a higher degree of dynamic variability than expected for this critical substructure... - Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynaminK M Ferguson
Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06510
Cell 79:199-209. 1994..This surface includes the position of the X-linked immunodeficiency mutation in the Btk PH domain and may serve as a ligand-binding surface... - The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulationJ A Hirsch
Howard Hughes Medical Institute, Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511, USA
Cell 97:257-69. 1999..In conjunction with biochemical and mutagenesis data, we propose a molecular mechanism by which arrestin is activated for receptor binding... - Structure of NF-kappa B p50 homodimer bound to a kappa B siteG Ghosh
Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06510
Nature 373:303-10. 1995..The carboxy-terminal domains form a dimerization interface between beta-sheets using residues that are strongly conserved in the Rel family... - GTPase mechanism of Gproteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4J Sondek
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut
Nature 372:276-9. 1994..GTP gamma S, but also conserved residues for GTPase activity. Thus the Gt alpha.GDP.AIF-4.H2O structure provides new insight into the mechanism of GTP hydrolysis... - Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudateD L Scott
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511
Science 254:1007-10. 1991.... - The stereochemistry and biochemistry of the trp repressor-operator complexB F Luisi
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 66511
Biochim Biophys Acta 1048:113-26. 1990 - Crystallographic analysis of the interaction of the glucocorticoid receptor with DNAB F Luisi
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511
Nature 352:497-505. 1991..The DNA-induced dimer fixes the separation of the subunits' recognition surfaces so that the spacing between the half-sites becomes a critical feature of the target sequence's identity... - Purification and characterization of trp aporepressorA Joachimiak
Proc Natl Acad Sci U S A 80:668-72. 1983..Preliminary equilibrium dialysis experiments suggest that tryptophan binds to the aporepressor with a dissociation constant of 1.6 X 10(-5) M... - The three-dimensional structure of trp repressorR W Schevitz
Nature 317:782-6. 1985..The binding of L-tryptophan activates the aporepressor indirectly by fixing the orientation of the second helix of the helix-turn-helix motif and by moulding the details of the repressor's structure near the DNA binding surface... - The crystal structure of trp aporepressor at 1.8 A shows how binding tryptophan enhances DNA affinityR G Zhang
Nature 327:591-7. 1987..These flexible 'DNA-reading heads' flank a highly inflexible core domain formed by an unusual arrangement of interlocking alpha-helices from both subunits... - The DNA target of the trp repressorT E Haran
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511
EMBO J 11:3021-30. 1992.... - The structure of trp pseudorepressor at 1.65A shows why indole propionate acts as a trp 'inducer'C L Lawson
Department of Biochemistry and Molecular Biology, University of Chicago, Illinois 60637
Nature 333:869-71. 1988..This explains why IPA acts as an apparent trp inducer... - Crystal structure of trp repressor/operator complex at atomic resolutionZ Otwinowski
Department of Biochemistry and Molecular Biology, University of Chicago, Illinois 60637
Nature 335:321-9. 1988..Water-mediated polar contacts to the bases also appear to contribute part of the specificity... - Flexibility of the DNA-binding domains of trp repressorC L Lawson
Department of Biochemistry and Molecular Biology, University of Chicago, Illinois 60637
Proteins 3:18-31. 1988..This flexibility may be required by the various binding modes proposed for trp repressor in its search for and adherence to its three different operator sites... - Functional inferences from crystals of Escherichia coli trp repressorA Joachimiak
J Biol Chem 258:12641-3. 1983....