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Structure of Human C8 Protein Provides Mechanistic Insight into Membrane Pore Formation by Complement*
This is the first structure of a MAC family member and of a human MACPF-containing protein, and shows the modules in C8α and C8β are located on the periphery of C8 and not likely to interact with the target membrane, leading to a model of the MAC that explains how C8-C9 and C9-C 9 interactions could facilitate refolding and insertion of putative MACPF transmembrane β-hairpins to form a circular pore.
Crystal structure of the MACPF domain of human complement protein C8 alpha in complex with the C8 gamma subunit.
Expression, Purification and the 1.8 Å Resolution Crystal Structure of Human Neuron Specific Enolase
Characterization and inactivation of an agmatine deiminase from Helicobacter pylori.
The R163K mutant of human thymidylate synthase is stabilized in an active conformation: structural asymmetry and reactivity of cysteine 195.
An hTS variant is designed and expressed, R163K, in which the inactive conformation is destabilized, suggesting that at least one-third of hTS populates the active conformer, as judged by its oxidation state.
Fluoride inhibition of enolase: crystal structure and thermodynamics.
The crystal structure of the human neuronal enolase-Mg2F2P(i) complex (enolase fluoride/phosphate inhibitory complex, EFPIC) determined shows that the combination of anions effectively mimics an intermediate state in catalysis.
Structures of thiolate- and carboxylate-ligated ferric H93G myoglobin: models for cytochrome P450 and for oxyanion-bound heme proteins.
This investigation affords the first structural evidence that nonimidazole exogenous ligands bind in the proximal ligation site of the ferric H93G Mb cavity mutant, which has already been shown to be a versatile model system for the study of ligand binding to heme proteins.
Structures of asymmetric complexes of human neuron specific enolase with resolved substrate and product and an analogous complex with two inhibitors indicate subunit interaction and inhibitor…
Structure of human thymidylate synthase under low-salt conditions.
- L. Lovelace, W. Minor, L. Lebioda
- Chemistry, Materials ScienceActa crystallographica. Section D, Biological…
- 1 May 2005
The low-salt conditions of these crystals should be much more suitable for the study of thymidylate synthase inhibitors, especially those that utilize sulfate-binding sites to stabilize the inactive conformation of loop 181-197.
Replacement of Val3 in human thymidylate synthase affects its kinetic properties and intracellular stability .
Observations show that the N-terminal extension affects the conformational state of the hTS catalytic region, and each of the mechanisms leading to the high K(m,app) values can be exploited to facilitate design of compounds acting as allosteric inhibitors of hTS.