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Structural basis of water-specific transport through the AQP1 water channel
The analysis of the AQP1 pore indicates that the transport of protons through this channel is highly energetically unfavourable, and residues of the constriction region, in particular histidine 182, which is conserved among all known water-specific channels, are critical in establishing water specificity.
Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex.
Refined crystal structures of the 11-subunit bc1 complex from bovine heart reveal full views of this bifunctional enzyme, and the "Rieske" iron-sulfur protein subunit shows significant conformational changes in different crystal forms, suggesting a new electron transport mechanism of the enzyme.
Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution.
The three-dimensional structure of the proteasome from the archaebacterium Thermoplasma acidophilum has been elucidated by x-ray crystallographic analysis by means of isomorphous replacement and
Molecular design of aquaporin-1 water channel as revealed by electron crystallography
The electron crystallographic structure of the aquaporin-1 water channel, determined at approximately 6A, reveals that the protein has six transmembrane alpha-helices forming a trapezoid-like
Structure of the osmo-regulated H2O-channel, AQP-CHIP, in projection at 3.5 A resolution.
  • B. Jap, H. Li
  • Chemistry, Medicine
    Journal of molecular biology
  • 18 August 1995
An osmo-regulated H2O-channel, aquaporin-CHIP, from bovine red blood cell membranes was purified and reconstituted with lipids, forming two-dimensional crystalline patches that diffract to about 3.0 A resolution, confirming that the osmi-regulated basic packing unit is a tetramer and begins to reveal it's structural design.
CD147 is a regulatory subunit of the gamma-secretase complex in Alzheimer's disease amyloid beta-peptide production.
The purification of the native gamma-secretase complexes from HeLa cell membranes and the identification of an additional gamma- secretase complex subunit, CD147, a transmembrane glycoprotein with two Ig-like domains are reported, indicating that the presence of the CD147 subunit within the gamma-Secretase complex down-modulates the production of Abeta-peptides.
2D crystallization: from art to science.
The techniques as well as the principles of the 2D crystallization of membrane and water-soluble proteins for electron crystallography are reviewed. First, the biophysics of the interactions between
Structural studies of the transmembrane C-terminal domain of the amyloid precursor protein (APP): does APP function as a cholesterol sensor?
It is proposed that APP may serve as a cellular cholesterol sensor that is linked to mechanisms for suppressing cellular cholesterol uptake, and may be critical for the trafficking of these proteins to cholesterol-rich membrane domains, which leads to cleavage by beta- and gamma-secretase and resulting amyloid-beta production.
Protein 4.1R core domain structure and insights into regulation of cytoskeletal organization
The crystal structure of the core domain (N-terminal 30 kDa domain) of cytoskeletalprotein 4.1R has been determined and shows a cloverleaf-like architecture, in which the three lobes bind with three membrane associated proteins, and the location of calmodulin binding sites provide insight into how the protein 4.2R dynamically regulates cell shape in response to changes in intracellular Ca2+ levels.
Crystal structures of the Rhodococcus proteasome with and without its pro-peptides: implications for the role of the pro-peptide in proteasome assembly.
Structures of the Rhodococcus proteasome and a mutant form that prevents the autocatalytic removal of its pro-peptides reveal that the pro- peptide acts as an assembly-promoting factor by linking its own beta-subunit to two adjacent alpha-subunits, thereby providing a molecular explanation for the observed kinetics of proteasomes assembly.