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The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1
The three-dimensional structure of prostaglandin H2 synthase-1, an integral membrane protein, has been determined at 3.5 Å resolution by X-ray crystallography. This bifunctional enzyme comprisesExpand
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The structural basis of aspirin activity inferred from the crystal structure of inactivated prostaglandin H2 synthase
Aspirin exerts its anti-inflammatory effects through selective acetylation of serine 530 on prostaglandin H2 synthase (PGHS). Here we present the 3.4 Å resolution X-ray crystal structure of PGHSExpand
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An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel β-fibrils
  • A. E. Bevivino, P. Loll
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences…
  • 25 September 2001
The protein ataxin-3 contains a polyglutamine region; increasing the number of glutamines beyond 55 in this region gives rise to the neurodegenerative disease spinocerebellar ataxia type 3. ThisExpand
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Crystal Structure of a Josephin-Ubiquitin Complex
The Josephin domain is a conserved cysteine protease domain found in four human deubiquitinating enzymes: ataxin-3, the ataxin-3-like protein (ATXN3L), Josephin-1, and Josephin-2. Josephin domainsExpand
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Structural analysis of NSAID binding by prostaglandin H2 synthase: time-dependent and time-independent inhibitors elicit identical enzyme conformations.
Nonsteroidal antiinflammatory drugs (NSAIDs) block prostanoid biosynthesis by inhibiting prostaglandin H(2) synthase (EC 1.14.99.1). NSAIDs are either rapidly reversible competitive inhibitors orExpand
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Membrane protein structural biology: the high throughput challenge.
  • P. Loll
  • Biology, Medicine
  • Journal of structural biology
  • 1 April 2003
Membrane proteins represent roughly one-third of the proteins encoded in the genome, yet fewer than 1% of the proteins are of known structure. High-throughput crystallography offers the hope ofExpand
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Colicin occlusion of OmpF and TolC channels: outer membrane translocons for colicin import.
The interaction of colicins with target cells is a paradigm for protein import. To enter cells, bactericidal colicins parasitize Escherichia coli outer membrane receptors whose physiological purposeExpand
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First structure of full-length mammalian phenylalanine hydroxylase reveals the architecture of an autoinhibited tetramer
Significance Phenylketonuria and milder hyperphenylalaninemias constitute the most common inborn error of amino acid metabolism, usually caused by defective phenylalanine hydroxylase (PAH). AlthoughExpand
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Simultaneous Recognition of a Carboxylate-Containing Ligand and an Intramolecular Surrogate Ligand in the Crystal Structure of an Asymmetric Vancomycin Dimer
Vancomycin is one of the most important and commonly used antibiotics in hospitals. Despite numerous investigations, however, it is not clear how vancomycin recognizes its site of action in theExpand
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Ligation independent cloning vectors for expression of SUMO fusions.
With demand increasing for the production of many different proteins for biophysical or biochemical analyses, rapid methods are needed for the cloning, expression and purification of nativeExpand
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