Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Gertraud Koellner"'
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 60:1417-1424
Purine-nucleoside phosphorylase (PNP) deficiency in humans leads to inhibition of the T-cell response. Potent membrane-permeable inhibitors of this enzyme are therefore considered to be potential immunosuppressive agents. The binary complex of the tr
Publikováno v:
Nucleosides, Nucleotides and Nucleic Acids. 22:1699-1702
The crystal structure at 2.05 A resolution of calf spleen PNP complexed with stoichiometric concentration of acyclic nucleoside phosphonate inhibitor, 2,6-diamino-(S)-9-[2-(phosphonomethoxy)propyl]purine, in a new space group P2(1)2(1)2(1) which cont
Publikováno v:
Nucleosides, Nucleotides and Nucleic Acids. 22:1695-1698
Binding enthalpies, dissociation constants and stoichiometry of binding for interaction of trimeric calf spleen and Cellulomonas sp. purine nucleoside phosphorylases with their ground state analogues (substrates and inhibitors) were studied by calori
Autor:
Agnieszka Bzowska, Wolfram Saenger, Marija Luić, Gertraud Koellner, Janusz Stepinski, Beata Wielgus-Kutrowska, Thomas Steiner
Publikováno v:
Journal of Molecular Biology. 315:351-371
The crystal structure of the ternary complex of hexameric purine nucleoside phosphorylase (PNP) from Escherichia coli with formycin A derivatives and phosphate or sulphate ions is determined at 2.0 Angstrom resolution. The hexamer is found as a trime
Autor:
Gertraud Koellner, Thomas Steiner
Publikováno v:
Journal of Molecular Biology. 305:535-557
A comprehensive structural analysis of X--H...pi hydrogen bonding in proteins is performed based on 592 published high-resolution crystal structures (< or = 1.6 A). All potential donors and acceptors are considered, including acidic C--H groups. The
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 57:30-36
The calf spleen purine nucleoside phosphorylase (PNP) ternary complex with an N(7)-acycloguanosine inhibitor and a phosphate ion has been crystallized in the cubic space group P2(1)3, with unit-cell parameter a = 94.11 Angstrom and one monomer per as
Autor:
Charles B. Millard, Thomas Steiner, Israel Silman, Gertraud Koellner, Joel L. Sussman, Gitay Kryger
Publikováno v:
Journal of Molecular Biology. 296:713-735
Buried water molecules and the water molecules in the active-site gorge are analyzed for five crystal structures of acetylcholinesterase from Torpedo californica in the resolution range 2.2-2.5 A (native enzyme, and four inhibitor complexes). A total
Autor:
Antoine M. M. Schreurs, Thomas Steiner, Gertraud Koellner, R. Srinivasan, Kathavarayan Subramanian, S. Suresh Kumar, K. Rajagopalan, Jan Kroon
Publikováno v:
Journal of Molecular Structure. 448:51-55
In the crystal structure of N-(4-methylphenyl)-N-prop-2-ynylurea, urea dimers are formed which are linked by cooperative NH···CCH···O hydrogen bonds, leading to an infinite two-dimensional hydrogen bond network.
Publikováno v:
Journal of Molecular Structure. 444:21-27
The X-ray crystal structure of 2-chloro-2′-deoxyadenosine was determined at low temperature [space group orthorhombic P21212, a = 7.493(6), b = 16.894(4), c = 9.065(4) →A, V = 1147.6(11) →A3, 4097 unique reflections, R = 0.050]. The ribose unit
Publikováno v:
Journal of Chemical Crystallography. 28:149-152
The X-ray crystal structure of 1,6-bis(N-cyano-p-methoxy-anilino)-2,4-hexadiyne, C22H18N4O2, is determined. The crystal packing is dominated by phenyl stacking interactions. Weak C–H···N hydrogen bonds help align the molecules. C–H···π hyd