117815253
Higgs Boson Searches with ATLAS based on 2010 Data
The results of Higgs Boson searches with the ATLAS detector based on 2010 proton proton collision data corresponding to integrated luminosities of up to 39 pb-1are presented. Searches for H --> 2 photons, H --> W+W- --> l+l- 2 neutrinos and H --> ZZ --> l+l- 2 neutrinos / l+l- qqbar in the context of the Standard Model (SM), for H--> tau+ tau- in the context of the Minimal Supersymmetric Extension of the Standard Model (MSSM) and for a generic scalar at low mass in the vicinity of the Ypsilon resonance decaying to a pair of muons are discussed. All observations are in agreement with the expectations from the background-only hypothesis. Hence exclusion limits at 95% confidence level are derived
117172015
The Higgs Boson: Still Elusive After 40 Years
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.
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.
122077797
SEARCHES FOR NEW PHYSICS AT LEP
2506186
Model-independent determination of the top Yukawa coupling from LHC and ILC
We show how a measurement of the process pp→tt̄H0+X at the Large Hadron Collider (LHC) and a measurement of the Higgs boson branching ratios BR(H0→bb̄) and BR(H0→W+W-) at a future linear electron positron collider (ILC) can be combined to extract a value of the top quark Yukawa coupling in a model-independent way. We find that for masses with 120 GeV/c2<mH<200 GeV/c2 a measurement precision of 15% including systematic uncertainties can be achieved for integrated luminosities of 300 fb-1 at the LHC and 500 fb-1 at the ILC at a centre-of-mass energy of 350 GeV. 
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.
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.
29559148
Structural basis for the recognition of a bisphosphorylated MAP kinase peptide by human VHR protein Phosphatase.
Human VHR (vaccinia H1 related phosphatase) is a member of the dual-specificity phosphatases (DSPs) that often act on bisphosphorylated protein substrates. Unlike most DSPs, VHR displays a strong preference for dephosphorylating phosphotyrosine residues over phosphothreonine residues. Here we describe the 2.75 A crystal structure of the C124S inactive VHR mutant in complex with a bisphosphorylated peptide corresponding to the MAP kinase activation lip. This structure and subsequent biochemical studies revealed the basis for the strong preference for hydrolyzing phosphotyrosine within bisphosphorylated substrates containing -pTXpY-. In the structure, the two phospho residues are oriented into distinct pockets; the phosphotyrosine is bound in the exposed yet deep active site cleft while the phosphothreonine is loosely tethered into a nearby basic pocket containing Arg(158). As this structure is the first substrate-enzyme complex reported for the DSP family of enzymes, these results provide the first glimpse into how DSPs bind their protein substrates.
17287147
Structural Basis of Core Promoter Recognition in a Primitive Eukaryote
Transcription start site selection in eukaryotes is mediated through combinations of the TATA, initiator (Inr), and downstream promoter elements (DPE). In Trichomonas vaginalis, a parabasalian flagellate thought to represent an ancient eukaryote lineage, the Inr appears to be solely responsible for start site selection and is recognized by the initiator binding protein 39 kDa (IBP39). IBP39 contains an N-terminal Inr binding domain (IBD) connected via a flexible linker to a C-terminal domain (C domain). Here we present crystal structures of the apoIBD and IBD-Inr complexes and the C domain. The IBD structures reveal a winged-helix motif with prokaryotic and eukaryotic features and a scaffold similar to that of ETS-family proteins. The C domain structure and biochemical studies indicate that it interacts with the T. vaginalis RNAP II large subunit C-terminal domain. These data suggest that binding of IBP39 to the Inr directly recruits RNAP II and in this way initiates transcription.
38152937
Structural Mechanisms of QacR Induction and Multidrug Recognition
The Staphylococcus aureus multidrug binding protein QacR represses transcription of the qacA multidrug transporter gene and is induced by structurally diverse cationic lipophilic drugs. Here, we report the crystal structures of six QacR-drug complexes. Compared to the DNA bound structure, drug binding elicits a coil-to-helix transition that causes induction and creates an expansive multidrug-binding pocket, containing four glutamates and multiple aromatic and polar residues. These structures indicate the presence of separate but linked drug-binding sites within a single protein. This multisite drug-binding mechanism is consonant with studies on multidrug resistance transporters.