Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction
Article Abstract:
A protein involved in membrane trafficking and signal transduction, Hrs, has been investigated. The 2-angstrom X-ray structure of the 219-residue N-terminal VHS and FYVE tandem domains has been determined. The structure made up of the two domains constitutes an exact 2-fold-related homodimer by means of antiparallel association of FYVE domains, in the main.
author: Nickitenko, Alexei, Mao, Yuxin, Duan, Xiaoqun, Lloyd, Thomas E., Wu, Xiaoqun, Bellen, Hugo, Quiocho, Florante A.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2000
Research, Cellular signal transduction, Biological transport, Cytochemistry, Cellular control mechanisms, Cell regulation, Protein structure
A novel all helix fold of the AP180 amino-terminal domain for phosphoinositide binding and clathrin assembly in synaptic vesicle endocytosis
Article Abstract:
Research has been conducted on the clathrin-mediated endocytosis. The role of this endocytosis in retrieving synaptic vehicles from the plasma membrane following exocytosis has been investigated and the results are presented.
author: Mao, Yuxin, Quiocho, Florante A., Chen Jue, Maynard, Jennifer A., Zhang, Bing
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2001
Statistical Data Included, Cell research, Cytological research, Amines, Endocytosis, Exocytosis, Phosphoinositides, Phosphatidylinositols, Clathrin
Crystal structure of Pl-Scel, a homing endonuclease with protein splicing activity
Article Abstract:
The crystal structure of the the yeast PI-Scel bifunctional protein was analyzed at 2.4 angstrom resolution to characterize the structure-function relationships of the protein. Analysis of the crystal structure of the yeast PI-Scel indicated the presence of a highly conserved amino acid residue in the nucleolytic active site. The bifunctional yeast protein also exhibited structural-functional duality and acted as a monomeric endonuclease.
author: Duan, Xiaoqun, Quiocho, Florante A., Gimble, Frederick S.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
Enzymes, Enzyme structure-activity relationships, Protein conformation, Restriction enzymes, DNA, DNA restriction enzymes
subjects list: United States, Physiological aspects, Proteins, Cell membranes, Plasma membranes, Analysis
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