The Claim
The human creatine transporter (hCRT) exhibits a canonical LeuT-fold structural architecture composed of 12 transmembrane helices organized into two pseudosymmetric inverted repeats, which provides the structural basis for substrate and sodium ion binding within the neurotransmitter sodium symporter family.
What the research says
Not yet evaluated
We are still looking at what the research says.
These are independent scores, not a percentage. Higher-grade studies count more, so a single strong opposing study can outweigh several weaker ones.
The protein that moves creatine in human cells has a specific 3D shape made of 12 spiral sections, and this shape helps it grab creatine and sodium like a lock and key.
See the scientific wording
The human creatine transporter (hCRT) adopts a canonical LeuT-fold structure with 12 transmembrane helices arranged in two pseudosymmetric inverted repeats, which serves as the structural framework for substrate and ion binding in this neurotransmitter sodium symporter family.
What the research says
1 studyThe study took detailed pictures of the creatine transporter in human cells and found it has the exact shape described in the claim, with 12 helices folded in a specific, well-known pattern.
Score breakdown, mechanism chain, raw evidence, ideal studies needed & 1 supporting studies
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