Fig. 4: Stomatin β-barrel domain forms a central hydrophobic portal at the narrow end.
From: Structural basis for membrane microdomain formation by a human Stomatin complex
a Cytosolic view of the Stomatin 16-mer showing the C-terminal β-barrel assembly at the narrow end. Each subunit contributes one β-strand, forming a closed circular structure. b Zoom-in of the β-barrel viewed from the cytosolic side. The central pore has an inner diameter of ~1.8 nm, suggesting possible selective diffusion of small molecules or ions. c Side view of the β-barrel structure rotated 90°, showing alternating strands from Conformer A and Conformer B. Conserved residues line the inner surface, forming a hydrophobic core. Residues from each conformer are color-coded and labeled to show side chain organization around the pore.
