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The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2.
The three-dimensional structure of mouse ribonucleotide reductase R2 has been determined at 2.3 A resolution using molecular replacement and refined to an R-value of 19.1% (Rfree = 25%) with good…
Crystal structure of tetranectin, a trimeric plasminogen‐binding protein with an α‐helical coiled coil
Tyr702 Is an Important Determinant of Agonist Binding and Domain Closure of the Ligand-Binding Core of GluR2
The results show that the selectivity of (S)-CPW399 toward full-length GluR2 relative to GLUR3 is reflected in the binding data on the two soluble constructs, allowing the use of (Y702F)GluR 2-S1S2J as a model system for studying Glu R2/Glu R3 selectivity.
Crystal structure of a partly self-complementary peptide nucleic acid (PNA) oligomer showing a duplex-triplex network.
- B. Petersson, B. B. Nielsen, J. Kastrup
- ChemistryJournal of the American Chemical Society
- 9 February 2005
The structural diversity of this PNA demonstrates how the PNA backbone is able to adapt to structures governed by the stacking and hydrogen-bonding interactions between the nucleobases.
Structure of the C-type lectin carbohydrate recognition domain of human tetranectin.
- J. Kastrup, B. B. Nielsen, I. K. Larsen
- ChemistryActa crystallographica. Section D, Biological…
- 1 September 1998
The crystal structure of the carbohydrate recognition domain (CRD) of human TN (TN3) has been determined separately at 2.0 A resolution in order to obtain detailed information on the two calcium binding sites, essential for the elucidation of the specificity of TN towards oligosaccharides.
1,8-Naphthyridin-2(1H)-ones. Novel Bicyclic and Tricyclic Analogues of Thymine in Peptide Nucleic Acids (PNAs)
Compound bT is shown to be an effective mimic of the natural thymine nucleobase in Pna-DNA, PNA-RNA, and PNA -PNA duplex structures and tricyclic derivative tC in place of cytosine in PNA oligomers increased the thermal stability and the sequence specificity was diminished in some PNA's duplex systems.
Exploring the GluR2 ligand‐binding core in complex with the bicyclical AMPA analogue (S)‐4‐AHCP
The X‐ray structure of the ionotropic GluR2 ligand‐binding core in complex with the bicyclical AMPA analogue (S)‐2‐amino‐3‐(3‐hydroxy‐7,8‐dihydro‐6H‐cyclohepta[d]‐4‐isoxazolyl)propionic acid and the binding pharmacology of this construct and of the full‐length GLUR2 receptor have been determined.
Tyr 702 Is an Important Determinant of Agonist Binding and Domain Closure of the Ligand-Binding Core of GluR 2
Ionotropic glutamate receptors mediate most rapid excitatory synaptic transmission in the mammalian central nervous system, and their involvement in neurological diseases has stimulated widespread…
Crystallization and crystallographic investigations of the small subunit of mouse ribonucleotide reductase
Structures of two ribonucleotide reductase inhibitors: 1-hydroxy-1-methylurea and 1-hydroxy-3-methylurea
The conformation of O-N-C=O in both 1-hydrosy- 1-methylurea and 1-hydrosy-3-methylurea is antiperiplanar and is stabilized by intramolecular NH---O hydrogen bonding. Pyramidalization of the N atom…