Showing papers in "Structure in 2002"

TL;DR: The crystal structure of the bovine 20S proteasome is determined at 2.75 A resolution and a model of the immunoproteasome was predicted from this constitutive structure.

TL;DR: This work provides an improved picture of the interactions between adjacent protofilaments, which are responsible for microtubule stability, and also suggests that some structural features are different in microtubules from those in the zinc sheets with which the tubulin structure was determined.

TL;DR: The crystal structures of complexes of an inactive variant of HIV-1 protease with six peptides that correspond to the natural substrate cleavage sites are solved, revealing an asymmetric shape rather than a particular amino acid sequence in this enzyme.

TL;DR: Although the eukaryotic and prokaryotic polypeptide release (translation termination) factors are functionally similar, they turn out to be very different in overall shape and architecture and in the location of key functional elements.

TL;DR: The crystal structures suggest a mechanism for ANS-catalyzed anthocyanidin formation from the natural leucoanthocyanIDin substrates involving stereoselective C-3 hydroxylation and provides a template for the ubiquitous family of plant nonhaem oxygenases for future engineering and inhibition studies.

TL;DR: The solution structure of the human lamin A/C C-terminal globular domain which contains specific mutations causing four different heritable diseases is determined and the consequences of the mutations causing muscle-specific diseases or lipodystrophy are clearly shown.

TL;DR: The structure of the PhoB effector domain in complex with its target DNA sequence, or pho box, reveals a novel tandem arrangement in which several monomers bind head to tail to successive 11-base pair direct-repeat sequences, coating one face of a smoothly bent double helix.

TL;DR: The 2.7 A X-ray crystal structure of the HNF4gamma ligand binding domain (LBD) revealed the presence of a fatty acid within the pocket, with the AF2 helix in a conformation characteristic of a transcriptionally active nuclear receptor.

TL;DR: The first crystal structure of the ligand binding domain (LBD) of RORα, at 1.63 A resolution, is described, which suggests that ROR α could play a key role in the regulation of cholesterol homeostasis and thus represents an important drug target in cholesterol-related diseases.

TL;DR: The excised 28 kDa SrfTE domain, a member of the alpha/beta hydrolase enzyme family, exhibits a distinctive bowl-shaped hydrophobic cavity that hosts the acylpeptide substrate and tolerates its folding to form a cyclic structure and provides a basis for understanding the mechanism of acyl-PCP substrate recognition and for the cyclization reaction that results in release of the macrolactone cyclic heptapeptide.

TL;DR: The FAK and Aurora-A structures are the first determined within two unique subfamilies of human kinases, and all three structures provide new insights into kinase regulation and the design of selective inhibitors.

TL;DR: Manual docking of the substrate quercetin into the active site showed that the different geometries of the copper site might be of catalytic importance.

TL;DR: The structure of a complex with an AP-2 binding segment from amphiphysin reveals a novel binding motif that is also used by AP180 and the 170 kDa isoform of synaptojanin and can be found in several potential endocytic proteins, including HIP1, CD2AP, and PLAP.

TL;DR: The results provide a starting point for the rational design of new XDH inhibitors and reveal that the bacterial and bovine XDH have highly similar folds despite differences in subunit composition.

TL;DR: Crystal contacts show that peptides bind within the crevice, suggesting a model for chaperone activity whereby segments of polypeptide may be repetitively sequestered and released during the membrane protein-folding process.

TL;DR: Biochemical analysis of bacterial and human Obg proteins combined with theStructural analysis of Bacillus subtilis Obg revealed respective domain architectures and how they are coupled through the putative switch elements of the C-terminal GTPase domain in apo and nucleotide-bound configurations.

TL;DR: The structural homology with E. coli FDH-H shows that the essential residues (SeCys158, His159, and Arg407) at the active site are conserved.

TL;DR: The structural resemblance with carbamate kinase and the alignment of the sequences suggest that NAGK is a structural and functional prototype for the amino acid kinase family, which differs from other acylphosphate-making devices represented by phosphoglycerate kinase, acetate kinases, and biotin carboxylase.

TL;DR: Structural and functional analyses of point mutants demonstrate that the compound and ligand binding regions are linked, suggesting that the PAS domain serves as a ligand-regulated switch for this eukaryotic signaling system.

TL;DR: The trajectory provides a unified dynamic description of the coupled subunit motions involved in the 120 degrees rotation cycles of F(1)-ATPase.

TL;DR: The structure of Tdp1 confirms that the protein has many similarities to the members of the phospholipase D (PLD) superfamily and indicates a similar catalytic mechanism and suggests how the unusual protein-DNA substrate binds and provides insights about the nature of the substrate in vivo.

TL;DR: Steady-state kinetic analysis demonstrates that autophosphorylation results in a 200-fold increase in k(cat) and a 10-fold decrease in the K(m) for ATP, and suggests that an additional in vivo component may contribute to regulation via the juxtamembrane region.

TL;DR: Because the continuous assignment reproduces the structural variation between many NMR models from one single model, functionally important variation can be extracted from a single X-ray structure.

TL;DR: This work has shown that the fundamental amyloid fibril folding motif remains unknown, and one model, based on the parallel beta helix, remains in the foreground of speculation on the molecular make-up of amyloids.

TL;DR: Heterooligomeric enzymes comprising homologous subunits in which one chain is catalytically inactive and enzyme polypeptides that contain internal catalytic and noncatalytic duplications of an ancient enzyme domain are discussed.

TL;DR: Several fold predictions, based in part on sequence repeats thought to match modular beta sheets, have been proved correct.

TL;DR: The epsilon subunit of the Escherichia coli replicative DNA polymerase III is the proofreading 3'-5' exonuclease, and structures were identical, except for differences in the way TMP and water molecules are coordinated to the binuclear metal center in the active site.

TL;DR: Methods developed here open up a direct avenue for exploration of the effects of pressure on proteins, and correlation with low-pH structures suggests observed structural changes are associated with global conformational substates.

TL;DR: In this article, the C-terminal focal adhesion targeting (FAT) domain was reported to have a FAT-like fold for CAS, Efs/Sin, and HEF1.

TL;DR: It is demonstrated that, in solution, CV-N can exist both in monomeric and in domain-swapped dimeric form, with mutation of the single proline residue in the hinge to glycine significantly stabilizes the protein in both its monomersic and dimeric forms.