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Conformational States of Human Rat Sarcoma (Ras) Protein Complexed with Its Natural Ligand GTP and Their Role for Effector Interaction and GTP Hydrolysis*
Ras in conformational state 2 has a higher affinity to effectors as well as a higher GTPase activity, which can be used to explain why many mutants have a low GTP enzyme activity but are not oncogenic. Expand
Growth and Thallus Morphogenesis of Ulva mutabilis (Chlorophyta) Depends on A Combination of Two Bacterial Species Excreting Regulatory Factors
The Roseobacter species exhibits a specific chemotactic affinity to the rhizoid cells of U. mutabilis and seems to cooperate with the Cytophaga strain and the alga by chemical communication forming a symbiotic tripartite community. Expand
Dynamic properties of the Ras switch I region and its importance for binding to effectors
The results indicate that minor changes in the switch region, such as removing the side chain methyl group of Thr-35, drastically affect dynamic behavior and, in turn, interaction with effectors. Expand
Fundamental link between folding states and functional states of proteins.
The supposed fundamental link using the Ras protein complexed with the GTP analogue GppNHp that occurs in two structural states coexisting in solution is demonstrated that state 1 represents the conformation interacting with guanine nucleotide exchange factors (GEFs). Expand
Perturbation of the conformational equilibria in Ras by selective mutations as studied by 31P NMR spectroscopy
31P NMR spectroscopy shows that the conformational equilibrium can be shifted specifically by point mutations, including mutations with oncogenic potential, thus modifying the effector interactions and their coupling to dynamic properties of the protein. Expand
Conformational states of Ras complexed with the GTP analogue GppNHp or GppCH2p: implications for the interaction with effector proteins.
The guanine nucleotide-binding protein Ras occurs in solution in two different states, state 1 and state 2, when the GTP analogue GppNHp is bound to the active center as detected by (31)P NMRExpand
Structural insights into the small G-protein Arl13B and implications for Joubert syndrome.
The crystal structure of Chlamydomonas rheinhardtii Arl13B, comprising the G-domain and part of its unique C-terminus, revealed an incomplete active site, and together with biochemical data the present study accounts for the absence of intrinsic GTP hydrolysis by this protein. Expand
A novel mechanism for the modulation of the Ras-effector interaction by small molecules.
With Zn(2+)-cyclen the authors found a small molecule which selectively stabilizes the weak-binding state and may serve as lead compound for the development of a new type of Ras-inhibitors. Expand
Metal-bis(2-picolyl)amine complexes as state 1(T) inhibitors of activated Ras protein.
The novel state (1T) inhibitor Zn(2+)-BPA (BPA = bis(2-picolyl)amine) binds outside the nucleotide binding pocket but nevertheless allosterically stabilizes state’1(T) and thus inhibits the Ras-Raf interaction. Expand