Showing papers in "Structure in 1994"

TL;DR: The structure of Candida antarctica lipase B shows that the enzyme has a Ser-His-Asp catalytic triad in its active site, which accounts for the substrate specificity and high degree of stereospecificity of this lipase.

TL;DR: The cofactor arrangement and the mode of binding to the protein seem to be very similar among the non-sulphur bacterial photosynthetic RCs, particularly along the electron transfer pathway.

TL;DR: The exceptionally high density of the protein interior shown here implies that packing forces play a more important role in protein stability than has been believed hitherto.

TL;DR: Structural and sequence comparisons indicate an evolutionary homology, albeit remote, between the glycoprotein hormone chains and other cystine-knot proteins, notably platelet-derived growth factor.

TL;DR: In this article, the structure of chitinase A from Serratia marcescens has been solved by multiple isomorphous replacement and refined at 2.3 A resolution, resulting in a crystallographic R-factor of 16.2%.

TL;DR: Structural comparisons between cAMP-dependentprotein kinase, cyclin-dependent kinase 2 and mitogen-activated protein kinase reveal which features are common to the protein kinases family and which are enzyme-specific.

TL;DR: The conformation of the two forms of antithrombin demonstrates the extraordinary mobility of the reactive loop in the serpins and provides insights into the folding of the loop required for inhibitory activity together with the potential modification of this by heparin.

TL;DR: The structure provides insight into the pathogenic mechanisms of pertussis toxin and the evolution of bacterial toxins, and knowledge of the tertiary structure of the active site forms a rational basis for elimination of catalytic activity in recombinant molecules for vaccine use.

TL;DR: Protein structure-based drug design is rapidly gaining momentum and the new opportunities, developments and results in this field are almost unbelievable compared with the situation less than a decade ago.

TL;DR: The carbohydrate-binding sites in MBP-A are too far apart for a single trimer to bind multivalently to a typical mammalian high-mannose oligosaccharide, and MBPs can recognize pathogens selectively by binding avidly only to the widely spaced, repetitive sugar arrays on pathogenic cell surfaces.

TL;DR: The large buried surface area and numerous polar interactions in the trimer indicate that this form of the knob protein is predominant in solution, suggesting a possible assembly pathway for the native fiber protein.

TL;DR: The recent determination of the structure of a class II MHC molecule complexed to a specific peptide reveals both similarities and differences with peptide binding by class I MHC as mentioned in this paper.

TL;DR: The structure of cy tochrome f allows prediction of the approximate docking site of plastocyanin and should allow systematic studies of the mechanism of intra- and inter-protein electron transfer between the cytochrome heme and plastOCyanin copper, which are approximately isopotential.

TL;DR: In FMDV type C, amino acid substitutions seen in mutants that are resistant to neutralization by monoclonal antibodies (MAbs) map to predominantly surface-oriented residues with solvent-accessible side-chains not involved in interactions with other amino acids, whereas residues which are accessible but not substituted are found to be more frequently involved in protein-protein interactions.

TL;DR: High-resolution solution structural studies of the two forms of Escherichia coli thioredoxin found only subtle conformational changes occur upon changing the oxidation state of the active site cysteines, including the positions of some side chains and in hydrogen bonding patterns in theactive site region.

TL;DR: This work shows that the striking spectral changes seen upon phenol binding are due to close physical association of the flavin and phenolate and suggests that if NADPH is its true substrate, then OYE has adopted NADPH dependence during evolution.

TL;DR: The structure of hevamine shows a completely new lysozyme/chitinase fold and represents a new class of polysaccharide-hydrolyzing (beta alpha)8-barrel enzymes.

TL;DR: The environment and coordination of the two zinc ions in A. proteolytica aminopeptidase strongly support the view that the two metal ions constitute a co-catalytic unit and play equivalent roles during catalysis.

TL;DR: The active site has many features in common with other viral and bacterial neuraminidases but, uniquely, has an essential Ca2+ ion which plays a crucial structural role.

TL;DR: The structure of the diabody is very similar to that which had been predicted by molecular modelling, and should be capable of bringing together two cells, such as in cell-targeted therapy.

TL;DR: The tyrosine phosphatase Syp structure has revealed that sequence specificity can extend across the five residues following the phosphotyrosine, and has shown how the SH2 domain's surface topography can be altered with resulting changes in specificity, while conserving the structure of the central core of the domain.

TL;DR: In this paper, the authors further refined the structure of the short-chain dehydrogenase with its cofactor, nicotinamide adenine dinucleotide (NAD), and solvent molecules, at the same resolution.

TL;DR: The results are useful for extrapolating functional results among the short-chain cytokines and growth hormone, and provide a foundation for similar characterization of other subfamilies, and show that the placement of polar residues at different buried positions in each protein complicates sequence comparisons.

TL;DR: The evolutionary pressure on barstar for rapid binding of barnase is so strong that glutamate is preferred over alanine at position 80, even though it does not directly interact with barnase in the complex and significantly destabilizes the inhibitor structure.

TL;DR: The three-dimensional structural comparison of thermophilic and mesophilic citrate synthases has permitted catalytic and substrate-binding residues to be tentatively assigned in the archaeal, thermophile enzyme, and has identified structural features that may be responsible for its thermostability.

TL;DR: The structure of CD59 is used, in combination with existing biochemical data, to identify residues that may be involved in C8 binding and the main features of the protein structure are two antiparallel beta-sheets, a short helix that packs against the three-stranded beta-sheet, and a carboxy-terminal region that, although lacking regular secondary structure, is well defined.

TL;DR: The observed structural polymorphism establishes that G-tetraplexes can adopt topologies which project distinctly different groove dimensions, G-Tetrad base edges and linker segments for recognition by, and interactions with, other nucleic acids and proteins.

TL;DR: The refined solution structure of Oxy-1.5 is reported, which forms a well-defined, symmetrical structure with ordered thymine loops and is compared with the previously published crystal structure of the same oligonucleotide.

TL;DR: Structural studies of cross-reacting antibodies of this type demonstrate the capacity of two different proteins to bind to the same target structure on a third protein need not be based on the existence of identical or homologous amino acid sequences within those proteins.

TL;DR: The structures of the reduced and oxidized states of the (C62A, C69A,C73A) mutant of human thioredoxin are very similar and the packing of side chains within the protein core is nearly identical, suggesting that subtle differences between the oxidized and reduced states can be reliably assessed and evaluated.