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Architecture and Membrane Interactions of the EGF Receptor
The authors' molecular dynamics simulations of membrane-embedded EGFR suggest that, in ligand-bound dimers, the extracellular domains assume conformations favoring dimerization of the transmembrane helices near their N termini, dimerized of the juxtamembrane segments, and formation of asymmetric (active) kinase dimers. Expand
Conformational Coupling across the Plasma Membrane in Activation of the EGF Receptor
It is concluded that EGF binding removes steric constraints in the extracellular module, promoting activation through N-terminal association of the transmembrane helices and promotes an antiparallel interaction between juxtamembrane segments and release of inhibition by the membrane. Expand
Two-state allosteric behavior in a single-domain signaling protein.
A strong correlation is found between phosphorylation-driven activation of the signaling protein NtrC and microsecond time-scale backbone dynamics and a dynamic population shift between two preexisting conformations as the underlying mechanism of activation. Expand
Mechanism for Activation of the EGF Receptor Catalytic Domain by the Juxtamembrane Segment
It is shown that the intracellular juxtamembrane segment of the receptor, known to potentiate kinase activity, is able to dimerize the kinase domains. Expand
Regulation of the transcriptional activator NtrC1: structural studies of the regulatory and AAA+ ATPase domains.
- Seok-Yong Lee, A. de la Torre, D. Yan, S. Kustu, B. T. Nixon, D. Wemmer
- Biology, Medicine
- Genes & development
- 15 October 2003
The first crystal structures of the ATPase domain of an activator, the NtrC1 protein from the extreme thermophile Aquifex aeolicus, are reported, which consists of a novel loop that projects from the middle of an alpha helix. Expand
Crystal structure of an activated response regulator bound to its target
The crystal structure of BeF3−-activated CheY from E. coli in complex with an N-terminal peptide derived from its target, FliM is determined and reveals that the first seven residues of the peptide pack against the β4-H4 loop and helix H4 of CheY in an extended conformation, whereas residues 8–15 form two turns of helix andPack against the H4-β5-H5 face. Expand
Stable fluorescent complexes of double-stranded DNA with bis-intercalating asymmetric cyanine dyes: properties and applications.
The synthesis, proof of structure, and the absorption and fluorescence properties of two new unsymmetrical cyanine dyes, thiazole orange dimer and oxazole yellow dimer are reported, which form highly fluorescent complexes with double-stranded DNA (dsDNA) with greater than 1000-fold fluorescence enhancement. Expand
The Mechanism of Linkage-Specific Ubiquitin Chain Elongation by a Single-Subunit E2
This work has discovered that the K11-specific Ube2S orients the donor ubiquitin through an essential noncovalent interaction that occurs in addition to the thioester bond at the E2 active site. Expand
A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase.
The result indicates that, contrary to previous proposals, pyrroloquinoline quinone is not the active site cofactor in mammalian copper amine oxidases, and suggests that this compound has a functional role at an enzyme active site. Expand
Structural characterization of the reaction pathway in phosphoserine phosphatase: crystallographic "snapshots" of intermediate states.
- Weiru Wang, Ho S. Cho, +6 authors Sung-Hou Kim
- Chemistry, Medicine
- Journal of molecular biology
- 31 May 2002
High-resolution structures of PSP from Methanococcus jannaschii are presented, which define the open state prior to substrate binding, the complex with phosphoserine substrate bound, and thecomplex with AlF3, a transition-state analog for the phospho-transfer steps in the reaction. Expand