Evidence that Interaction between Conserved Residues in Transmembrane Helices 2, 3, and 7 Are Crucial for Human VPAC1 Receptor Activation-Reference-Cited by-同舟云学术

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Evidence that Interaction between Conserved Residues in Transmembrane Helices 2, 3, and 7 Are Crucial for Human VPAC1 Receptor Activation

Published:2010-06-23 Issue:3 Volume:78 Page:394-401
ISSN:0026-895X
Container-title:Molecular Pharmacology
language:en
Short-container-title:Mol Pharmacol

Author:

Chugunov Anton O.,Simms John,Poyner David R.,Dehouck Yves,Rooman Marianne,Gilis Dimitri,Langer Ingrid

Publisher

American Society for Pharmacology & Experimental Therapeutics (ASPET)

Subject

Pharmacology,Molecular Medicine

Reference38 articles.

1. Protein Structure Prediction and Structural Genomics

2. Activation of the β2-Adrenergic Receptor Involves Disruption of an Ionic Lock between the Cytoplasmic Ends of Transmembrane Segments 3 and 6

3. Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors;Ballesteros;Methods Neurosci,2005

4. A knowledge-based scale for the analysis and prediction of buried and exposed faces of transmembrane domain proteins

5. High-Throughput Modeling of Human G-Protein Coupled Receptors: Amino Acid Sequence Alignment, Three-Dimensional Model Building, and Receptor Library Screening

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