An alternative N-terminal fold of the intestine-specific annexin A13a induces dimerization and regulates membrane-binding
KM McCulloch, I Yamakawa, DA Shifrin… - Journal of Biological …, 2019 - ASBMB
Annexin proteins function as Ca 2+-dependent regulators of membrane trafficking and repair
that may also modulate membrane curvature. Here, using high-resolution confocal imaging,
we report that the intestine-specific annexin A13 (ANX A13) localizes to the tips of intestinal
microvilli and determined the crystal structure of the ANX A13a isoform to 2.6 Å resolution.
The structure revealed that the N terminus exhibits an alternative fold that converts the first
two helices and the associated helix–loop–helix motif into a continuous α-helix, as stabilized …
that may also modulate membrane curvature. Here, using high-resolution confocal imaging,
we report that the intestine-specific annexin A13 (ANX A13) localizes to the tips of intestinal
microvilli and determined the crystal structure of the ANX A13a isoform to 2.6 Å resolution.
The structure revealed that the N terminus exhibits an alternative fold that converts the first
two helices and the associated helix–loop–helix motif into a continuous α-helix, as stabilized …
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