Structural insight into pre-B cell receptor function

The pre-B cell receptor (pre-BCR) serves as a checkpoint in B cell development. In the 2.7 angstrom structure of a human pre-BCR Fab-like fragment, consisting of an antibody heavy chain (HC) paired with the surrogate light chain, the "unique regions" of VpreB and lambda5 replace the complementarity-determining region 3 (CDR3) loop of an antibody light chain and appear to "probe" the HC CDR3, potentially influencing the selection of the antibody repertoire. Biochemical analysis indicates that the pre-BCR is impaired in its ability to recognize antigen, which, together with electron microscopic visualization of a pre-BCR dimer, suggests ligand-independent oligomerization as the likely signaling mechanism.     

A radio pulsar spinning at 716 Hz

We have discovered a 716-hertz eclipsing binary radio pulsar in the globular cluster Terzan 5 using the Green Bank Telescope. It is the fastest spinning neutron star found to date, breaking the 24-year record held by the 642-hertz pulsar B1937+21. The difficulty in detecting this pulsar, because of its very low flux density and high eclipse fraction (approximately 40% of the orbit), suggests that even faster spinning neutron stars exist. If the pulsar has a mass less than twice the mass of the Sun, then its radius must be constrained by the spin rate to be <16 kilometers. The short period of this pulsar also constrains models that suggest that gravitational radiation, through an r-mode (Rossby wave) instability, limits the maximum spin frequency of neutron stars.     

Transformation of a star into a planet in a millisecond pulsar binary

Millisecond pulsars are thought to be neutron stars that have been spun-up by accretion of matter from a binary companion. Although most are in binary systems, some 30% are solitary, and their origin is therefore mysterious. PSR J1719-1438, a 5.7-millisecond pulsar, was detected in a recent survey with the Parkes 64-meter radio telescope. We show that this pulsar is in a binary system with an orbital period of 2.2 hours. The mass of its companion is near that of Jupiter, but its minimum density of 23 grams per cubic centimeter suggests that it may be an ultralow-mass carbon white dwarf. This system may thus have once been an ultracompact low-mass x-ray binary, where the companion narrowly avoided complete destruction.     

Yeast cells provide insight into alpha-synuclein biology and pathobiology

Alpha-synuclein is implicated in several neurodegenerative disorders, such as Parkinson's disease and multiple system atrophy, yet its functions remain obscure. When expressed in yeast, alpha-synuclein associated with the plasma membrane in a highly selective manner, before forming cytoplasmic inclusions through a concentration-dependent, nucleated process. Alpha-synuclein inhibited phospholipase D, induced lipid droplet accumulation, and affected vesicle trafficking. This readily manipulable system provides an opportunity to dissect the molecular pathways underlying normal alpha-synuclein biology and the pathogenic consequences of its misfolding.     

大学物理实验课改革初探

阐述了物理实验课在物理教学中的地位及河北农业大学物理实验课教学中存在的问题，探讨了打破旧的物理实验教学体系，在实验内容、实验手段、实验成绩评定等方面进行改革的思路。     

Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis

Peptidoglycan glycosyltransferases (GTs) catalyze the polymerization step of cell-wall biosynthesis, are membrane-bound, and are highly conserved across all bacteria. Long considered the "holy grail" of antibiotic research, they represent an essential and easily accessible drug target for antibiotic-resistant bacteria, including methicillin-resistant Staphylococcus aureus. We have determined the 2.8 angstrom structure of a bifunctional cell-wall cross-linking enzyme, including its transpeptidase and GT domains, both unliganded and complexed with the substrate analog moenomycin. The peptidoglycan GTs adopt a fold distinct from those of other GT classes. The structures give insight into critical features of the catalytic mechanism and key interactions required for enzyme inhibition.     

Structural insight into the ion-exchange mechanism of the sodium/calcium exchanger

Sodium/calcium (Na(+)/Ca(2+)) exchangers (NCX) are membrane transporters that play an essential role in maintaining the homeostasis of cytosolic Ca(2+) for cell signaling. We demonstrated the Na(+)/Ca(2+)-exchange function of an NCX from Methanococcus jannaschii (NCX_Mj) and report its 1.9 angstrom crystal structure in an outward-facing conformation. Containing 10 transmembrane helices, the two halves of NCX_Mj share a similar structure with opposite orientation. Four ion-binding sites cluster at the center of the protein: one specific for Ca(2+) and three that likely bind Na(+). Two passageways allow for Na(+) and Ca(2+) access to the central ion-binding sites from the extracellular side. Based on the symmetry of NCX_Mj and its ability to catalyze bidirectional ion-exchange reactions, we propose a structure model for the inward-facing NCX_Mj.