menusearch results
results of search on CRYSTALLOGRAPHY JOURNALS ONLINE
18 citations found for Lubkowski, J
Search for Lubkowski, J in the World Directory of Crystallographers
Results 1 to 18, sorted by name:
crystallization papers
Preliminary crystallographic studies of synthetically prepared thymus and activation-regulated chemokine (TARC) in the triclinic, hexagonal and tetragonal systems are described.
research papers
Crystal structures of the thymus and activation-regulated chemokine (TARC) have been solved by molecular replacement in both the triclinic P1 and tetragonal P41 space groups, and refined to resolutions of 1.72 and 2.1 Å, respectively. Both structural forms and the structure determination are described.
research papers
The crystal structure of human monocyte chemoattractant protein 4 (MCP-4), a member of the CC chemokine family, has been determined at 1.70 Å resolution.
protein structure communications
A crystal structure of ligand-free human glutamate carboxypeptidase II refined to 1.65 Å resolution is reported. The structure provides insight into the active-site of the enzyme in its unliganded state.
research communications
A recombinant version of the lectin CGL from the sea mussel C. grayanus was expressed, purified and crystallized. The structure determined at 2.12 Å resolution indicated that this lectin is a member of the β-trefoil family.
research papers
The structures of the Y25F mutant of E. coli L-asparaginase and of native E. chrysanthemi L-asparaginase with quasi-enantiomorphic crystals obtained in the hexagonal space groups P6522 and P6122, respectively, are compared.
research papers
The X-ray crystallographic structure of Acinetobacter glutaminasificans glutaminase-asparaginase has been reinterpreted and refined to an R factor of 0.171 at 2.9 Å resolution.
research papers
The crystal structure of E. chrysanthemi L-asparaginase has been refined at 1.0 Å resolution, elucidating the atomic level details of one of the largest asymmetric units studied to date at this level of accuracy.
short communications
The structure of bovine pancreatic trypsin inhibitor has been solved in a new crystal form where protein molecules create a decameric assembly.
abstracts
abstracts
In this report we present our progress in the functional and structural studies of human interleukin 24 (hIL-24). Interleukins and interferons (cytokines) together with their cognate receptors form a `front-end' of convoluted signaling networks, responsible for an immune-response to the presence of various pathogens. Cytokines are subjected to vigorous research related to their role in human physiology and disease and potential therapeutic uses. After many years of intense studies, information on some of cytokines is absent or limited, partly because new members are still being identified as well as due to difficulties of generating significant amounts of active preparations. A sub-family of `IL-10-related cytokines' also called the cytokine receptor type 2 family (CRF2) comprises nine members. One of CRF2 members is interleukin 24 (IL-24). The most interesting biological feature of human IL-24 (hIL-24) is its tumor inhibitory activity, observed in vitro for several cancer cell lines. IL-24 signals through the receptor complex comprising the high-affinity chain (IL-22R1 or IL-20R1) and the secondary, low-affinity chain (IL-20R2). Structure of IL-24 is currently unknown, although it is expected to be similar to those of other members of the CRF2 family. However, in silica analysis indicates several differences in the molecule of IL-24 when compared to its close homologues. One of more interesting is lack of two canonical disulfide bonds, found in all other interleukins from the CRF2 family, due to missing needed Cys residues. While an alternative, unique disulfide bond in IL-24 is possible, the appropriate experimental evidence is missing. Native IL-24 is N-glycosylated. Although this modification appears dispensable for biological activity of related cytokines, its role in IL-24 is not clear. We have expressed insoluble hIL-24 in bacteria and refolded it subsequently into a soluble, functional form. The mass spectrometry analysis confirmed presence of a single disulfide bond. Our non-glycosylated variant of hIL-24 activates the cognate receptor as efficiently as commercial preparations from eukaryotic sources. We observed, however, that stability of refolded hIL-24 is somewhat compromised. Subsequently, we plan investigating the structural properties of this cytokine.
abstracts
short communications
The crystal structure of the plant-type asparaginase from E. coli, EcAIII, has been solved by molecular replacement and refined to a resolution of 1.65 Å. Sodium ion-binding sites have been identified that were not observed in other related enzymes. The structure of EcAIII helps to explain some of the differences between the substrate specificities of plant-type asparaginases and glycosylasparaginases.
abstracts
letters to the editor
access
abstracts
research papers
The crystallographic structures of asparaginases of class 1 (bacterial-type), class 2 (plant-type) and class 3 (Rhizobium etli-type) in the PDB are reviewed in order to identify and, if possible, correct any modeling errors, with the purpose of creating a reliable data set for further research, including the development of new antileukemic agents.
abstracts
