Salt Bridge Switching from Arg290/Glu167 to Arg290/ATP Promotes the Closed-to-Open Transition of the P2X2 Receptor-Reference-Cited by-同舟云学术

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Salt Bridge Switching from Arg290/Glu167 to Arg290/ATP Promotes the Closed-to-Open Transition of the P2X2 Receptor

Published:2012-10-05 Issue:1 Volume:83 Page:73-84
ISSN:0026-895X
Container-title:Molecular Pharmacology
language:en
Short-container-title:Mol Pharmacol

Author:

Hausmann Ralf,Günther Janka,Kless Achim,Kuhlmann Daniel,Kassack Matthias U.,Bahrenberg Gregor,Markwardt Fritz,Schmalzing Günther

Publisher

American Society for Pharmacology & Experimental Therapeutics (ASPET)

Subject

Pharmacology,Molecular Medicine

Reference50 articles.

1. Cysteine Scanning Mutagenesis (Residues Glu52–Gly96) of the Human P2X1 Receptor for ATP

2. Trimeric Architecture of Homomeric P2X2 and Heteromeric P2X1+2 Receptor Subtypes

3. Polar Residues in the Second Transmembrane Domain of the Rat P2X2 Receptor That Affect Spontaneous Gating, Unitary Conductance, and Rectification

4. Structure and dynamics of Escherichia coli chemosensory receptors. Engineered sulfhydryl studies

5. Thermal motions of surface α-helices in the d-galactose chemosensory receptor

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