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Structural and biophysical studies of human cystine have revealed the molecular mechanisms and conformational kinetics of proton-coupled lysosomal amino acid transport
Cystine disease is a rare genetic disorder caused
The new study, published Sept.
"This paper could build a model for how to combine these three areas as well as biochemical analysis to quickly narrow down the functional range of proteins and identify therapeutic strategies," said Glenn Millhauser, Distinguished Professor and Chair of Chemistry and Biochemistry at the University of California, Santa Cruz, who is also the corresponding author
Cysteine is a special transporter that plays a vital role
Abnormal accumulation of cystine can cause extensive damage to tissues and organs and can lead to kidney failure, muscle atrophy and other problems
"It's a rare disease, but it can be fatal, and if left untreated, people with cystine disease usually die
Cystine has a different
However, to understand the structural changes of cystine during transport, a DEER study
"With that, we can figure out the mechanisms by which cystine switches between different states, and we can narrow it down to determine which protein amino acids drive that transition
These new insights into the molecular mechanisms of cystine transport activity not only provide a more detailed understanding of the pathogenesis of cystine disease, but also provide a possible therapeutic strategy
Similar methods can be used to target other transporters
essay
Structure and mechanism of human cystine output source cystine
