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.
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Article Abstract:
Recent studies that have elucidated the structure of G proteins are bound to stimulate further researches as to the functions posed by these structures. Some interesting structural questions are the single cleavage site in the beta subunit despite the presence of several potential sites which may have to do with the way with which the loop exposes the site. Another is the use of WD repeats (amino acid sequences bounded by Trp-Asp) to form the propeller configuration, and the function of the propeller configuration.
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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.
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