Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor
Article Abstract:
A study was conducted to determine the crystal structure of a soluble form of human HFE, a major histocompatibility complex-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. The locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions were observed in the structure of HFE. Also, tight binding of soluble transferrin receptor (TfR) and HFE was demonstrated at the basic pH of the cell surface. Findings support previous demonstration that HFE, transferrin and TfR form a ternary complex.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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Regulation of membrane trafficking: structural insights from a Rab/effector complex
Article Abstract:
Rab proteins is a branch of the superfamily of small GTPases that are responsible for coordinating membrane trafficking in eukaryotic cells. Rab proteins coordinate vesicle translocation and organelle docking at particular fusion sites within the secretory pathway. They also regulate levels of neurotransmitter release in neurons. Rab proteins are able to do all these functions by interacting with a subset of effector proteins.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
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