10 research outputs found
ΠΠΎΡΠΈΡΡΠ°Ρ ΡΡΡΡΠΊΡΡΡΠ° ΠΏΡΠΎΠ΄ΡΠΊΡΠΎΠ² ΡΠ»Π΅ΠΊΡΡΠΎΡ ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΎΠ³ΠΎ ΡΠΈΠ½ΡΠ΅Π·Π° Π½Π° ΠΏΠ΅ΡΠ΅ΠΌΠ΅Π½Π½ΠΎΠΌ ΡΠΎΠΊΠ΅ Π½Π°Π½ΠΎΠ΄ΠΈΡΠΏΠ΅ΡΡΠ½ΡΡ ΠΎΠΊΡΠΈΠ΄ΠΎΠ² ΠΎΠ»ΠΎΠ²Π°
ΠΠ΅ΡΠΎΠ΄Π°ΠΌΠΈ ΡΠ»Π΅ΠΊΡΡΠΎΠ½Π½ΠΎΠΉ ΠΌΠΈΠΊΡΠΎΡΠΊΠΎΠΏΠΈΠΈ ΠΈ Π½ΠΈΠ·ΠΊΠΎΡΠ΅ΠΌΠΏΠ΅ΡΠ°ΡΡΡΠ½ΠΎΠΉ Π°Π΄ΡΠΎΡΠ±ΡΠΈΠΈ Π°Π·ΠΎΡΠ° ΠΈΠ·ΡΡΠ΅Π½Π° ΠΏΠΎΡΠΈΡΡΠ°Ρ ΡΡΡΡΠΊΡΡΡΠ° ΠΏΡΠΎΠ΄ΡΠΊΡΠΎΠ² ΡΠ»Π΅ΠΊΡΡΠΎΠ»ΠΈΠ·Π° ΠΌΠ΅ΡΠ°Π»Π»ΠΈΡΠ΅ΡΠΊΠΎΠ³ΠΎ ΠΎΠ»ΠΎΠ²Π° Π½Π° ΠΏΠ΅ΡΠ΅ΠΌΠ΅Π½Π½ΠΎΠΌ ΡΠΎΠΊΠ΅ ΠΏΡΠΎΠΌΡΡΠ»Π΅Π½Π½ΠΎΠΉ ΡΠ°ΡΡΠΎΡΡ. Π£ΡΡΠ°Π½ΠΎΠ²Π»Π΅Π½ΠΎ, ΡΡΠΎ ΠΏΡΠΎΠ΄ΡΠΊΡΡ ΡΠΈΠ½ΡΠ΅Π·Π° Ρ
Π°ΡΠ°ΠΊΡΠ΅ΡΠΈΠ·ΡΡΡΡΡ Π²ΡΡΠΎΠΊΠΈΠΌΠΈ Π·Π½Π°ΡΠ΅Π½ΠΈΡΠΌΠΈ ΡΠ΄Π΅Π»ΡΠ½ΠΎΠΉ ΠΏΠ»ΠΎΡΠ°Π΄ΠΈ ΠΏΠΎΠ²Π΅ΡΡ
Π½ΠΎΡΡΠΈ ΠΈ ΠΌΠ΅Π·Π°ΠΏΠΎΡΠΈΡΡΠΎΠΉ ΡΡΡΡΠΊΡΡΡΠΎΠΉ. ΠΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ ΡΡΠ΅Π΄Π½ΠΈΠΉ ΡΠ°Π·ΠΌΠ΅Ρ ΡΠ°ΡΡΠΈΡ Π²Π°ΡΡΠΈΡΡΠ΅Ρ Π² ΠΈΠ½ΡΠ΅ΡΠ²Π°Π»Π΅ 10β¦30 Π½ΠΌ
An intramembrane aromatic network determines pentameric assembly of Cys-loop receptors
Cys-loop receptors are pentameric ligand-gated ion channels (pLGICs) that mediate fast synaptic transmission. Here functional pentameric assembly of truncated fragments comprising the ligand-binding N-terminal ectodomains and the first three transmembrane helices, M1-M3, of both the inhibitory glycine receptor (GlyR) alpha 1 and the 5HT(3)A receptor subunits was found to be rescued by coexpressing the complementary fourth transmembrane helix, M4. Alanine scanning identified multiple aromatic residues in M1, M3 and M4 as key determinants of GlyR assembly. Homology modeling and molecular dynamics simulations revealed that these residues define an interhelical aromatic network, which we propose determines the geometry of M1-M4 tetrahelical packing such that nascent pLGIC subunits must adopt a closed fivefold symmetry. Because pLGIC ectodomains form random nonstoichiometric oligomers, proper pentameric assembly apparently depends on intersubunit interactions between extracellular domains and intrasubunit interactions between transmembrane segments
Real Time Measures of Prestin Charge and Fluorescence during Plasma Membrane Trafficking Reveal Sub-Tetrameric Activity
Characterization of SLCO5A1/OATP5A1, a Solute Carrier Transport Protein with Non-Classical Function
Homodimeric anoctamin-1, but not homodimeric anoctamin-6, is activated by calcium increases mediated by the P2Y1 and P2X7 receptors
Structure of a prokaryotic fumarate transporter reveals the architecture of the SLC26 family
The SLC26 family of membrane proteins combines a variety of functions within a conserved molecular scaffold. Its members, besides coupled anion transporters and channels, include the motor protein Prestin, which confers electromotility to cochlear outer hair cells. To gain insight into the architecture of this protein family, we characterized the structure and function of SLC26Dg, a facilitator of proton-coupled fumarate symport, from the bacterium Deinococcus geothermalis. Its modular structure combines a transmembrane unit and a cytoplasmic STAS domain. The membrane-inserted domain consists of two intertwined inverted repeats of seven transmembrane segments each and resembles the fold of the unrelated transporter UraA. It shows an inward-facing, ligand-free conformation with a potential substrate-binding site at the interface between two helix termini at the center of the membrane. This structure defines the common framework for the diverse functional behavior of the SLC26 family