122077797
SEARCHES FOR NEW PHYSICS AT LEP
6747128
Prospects for the measurement of the structure of the coupling of a Higgs boson to weak gauge bosons in weak boson fusion with the ATLAS detector
The prospects for the measurement of the tensor structure of the vertex between a standard model Higgs boson and two weak gauge bosons using the distribution of the azimuthal angles between the two tagging jets in the weak boson fusion channel are studied in a Monte Carlo analysis using the fast simulation of the ATLAS detector. The decay channels H→τ+τ-→ll+4ν, H→τ+τ-→lh+3ν at mH=120 GeV and H→W+W-→llνν at mH=160 GeV are used in the analysis. For a standard model Higgs boson it is found that purely anomalous couplings are expected to be excluded at a confidence level corresponding to 2σ or more at mH=120 GeV and more than 5σ at mH=160 GeV from 30 fb-1 of data. With a value of 1 roughly reproducing the standard model cross section for a purely anomalous coupling, the standard deviation in a measurement of a contribution of a CP even anomalous coupling in addition to the standard model coupling is estimated to be 0.20 at mH=120 GeV and 0.09 at mH=160 GeV.
117936692
TPC with GEM readout for TESLA
A Time Projection Chamber (TPC) is proposed as the main tracking device for the detector at the future e+e− linear accelerator now studied in Europe. The performance requirements and the basic design using a Gas Electron Multiplier (GEM) as the readout device are described. Some preliminary R&D results are discussed.
8372632
Investigation of the Discovery Potential for Higgs Bosons of the Minimal Supersymmetric Extension of the Standard Model (MSSM) with ATLAS
The discovery potential of the ATLAS experiment at the LHC for Higgs bosons of the MSSM is discussed. Several CP conserving and one CP violating benchmark scenario are investigated.
139488231
LC TPC R & D: A proposal to the DESY PRC
5803090
Structural basis for cooperative DNA binding by two dimers of the multidrug-binding protein QacR.
The Staphylococcus aureus multidrug-binding protein QacR represses transcription of the qacA multidrug transporter gene and is induced by multiple structurally dissimilar drugs. QacR is a member of the TetR/CamR family of transcriptional regulators, which share highly homologous N-terminal DNA-binding domains connected to seemingly non-homologous ligand-binding domains. Unlike other TetR members, which bind approximately 15 bp operators, QacR recognizes an unusually long 28 bp operator, IR1, which it appears to bind cooperatively. To elucidate the DNA-binding mechanism of QacR, we determined the 2.90 A resolution crystal structure of a QacR-IR1 complex. Strikingly, our data reveal that the DNA recognition mode of QacR is distinct from TetR and involves the binding of a pair of QacR dimers. In this unique binding mode, recognition at each IR1 half-site is mediated by a complement of DNA contacts made by two helix-turn-helix motifs. The inferred cooperativity does not arise from cross-dimer protein-protein contacts, but from the global undertwisting and major groove widening elicited by the binding of two QacR dimers.
205016620
Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin
Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming α-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through the CaM-binding domain (CaMBD), which is located in an intracellular region of the α-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. Here we report the 1.60 Å crystal structure of the SK channel CaMBD/Ca2+/CaM complex. The CaMBD forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three α-helices, two from one CaMBD subunit and one from the other. As only the CaM N-lobe has bound Ca2+, the structure provides a view of both calcium-dependent and -independent CaM/protein interactions. Together with biochemical data, the structure suggests a possible gating mechanism for the SK channel.
22785877
Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein.
In prokaryotes, Hfq regulates translation by modulating the structure of numerous RNA molecules by binding preferentially to A/U-rich sequences. To elucidate the mechanisms of target recognition and translation regulation by Hfq, we determined the crystal structures of the Staphylococcus aureus Hfq and an Hfq-RNA complex to 1.55 and 2.71 A resolution, respectively. The structures reveal that Hfq possesses the Sm-fold previously observed only in eukaryotes and archaea. However, unlike these heptameric Sm proteins, Hfq forms a homo-hexameric ring. The Hfq-RNA structure reveals that the single-stranded hepta-oligoribonucleotide binds in a circular conformation around a central basic cleft, whereby Tyr42 residues from adjacent subunits stack with six of the bases, and Gln8, outside the Sm motif, provides key protein-base contacts. Such binding suggests a mechanism for Hfq function.
19913942
Crystal Structures of QacR-Diamidine Complexes Reveal Additional Multidrug-binding Modes and a Novel Mechanism of Drug Charge Neutralization*
The Staphylococcus aureus multidrug-binding protein QacR represses transcription of the plasmid-encoded membrane protein QacA, a multidrug efflux transporter. QacR is induced by multiple structurally dissimilar monovalent and bivalent cationic lipophilic compounds, many of which are effluxed from the cell by QacA via the proton motive force. The multidrug-binding pocket of QacR has been shown to be quite extensive and features several glutamates and multiple aromatic residues. To date, the structure of only one QacR-bivalent cationic drug complex (that of QacR bound to dequalinium) has been determined, and how other longer or shorter bivalent cationic compounds bind is unknown. Here we report the crystal structures of QacR bound to two cytotoxic bivalent diamidines, pentamidine and hexamidine. These compounds are structurally similar, differing by only one methylene carbon in the alkyl chain linker. However, this small difference results in very dissimilar binding modes. Similar to dequalinium, hexamidine spans the multidrug-binding pocket, and its positively charged benzamidine groups are neutralized by residues Glu-57 and Glu-120. Pentamidine binds QacR in a novel fashion whereby one of its benzamidine groups interacts with residue Glu-63, and the other is neutralized by carbonyl and side chain oxygen atoms. Thus, these structures demonstrate that a formal negative charge is not a prerequisite for binding positively charged drugs and underscore the versatility of the QacR and, likely, all multidrug-binding pockets.
837237
Crystal structures of apocalmodulin and an apocalmodulin/SK potassium channel gating domain complex.
Small conductance Ca2+-activated K+ channels (SK channels) are composed of the pore-forming alpha subunit and calmodulin (CaM). CaM binds to a region of the alpha subunit called the CaM binding domain (CaMBD), located intracellular and immediately C-terminal to the inner helix gate, in either the presence or absence of Ca2+. SK gating occurs when Ca2+ binds the N lobe of CaM thereby transmitting the signal to the attached inner helix gate to open. Here we present crystal structures of apoCaM and apoCaM/SK2 CaMBD complex. Several apoCaM crystal forms with multiple (12) packing environments reveal the same EF hand domain-swapped dimer providing potentially new insight into CaM regulation. The apoCaM/SK2 CaMBD structure, combined with our Ca2+/CaM/CaMBD structure suggests that Ca2+ binding induces folding and dimerization of the CaMBD, which causes large CaMBD-CaM C lobe conformational changes, including a >90 degrees rotation of the region of the CaMBD directly connected to the gate.