Sequence alignments
Alignments with generic residue numbers and residue plots.
G protein couplings
Unified coupling atlas and G protein selectivity profiles.
Structures
G protein structure statistics and browser with unique annotation.
Structure models
GPCR-G protein structure models.
G protein structure interface
Structure based coupling interface interactions.
GproteinDb
GproteinDb (G protein database) offers:
- Reference data (see Data box)
- Analysis tools (browse menu)
- Visualization (e.g., snakeplots)
- Experiment design (Coupling determinant mutations)
- Data deposition (for G protein couplings and interface mutations)
G proteins are the main mediators of GPCR signaling1.
Their activation is followed by recruitment of arrestins that arrest (stop) signaling or scaffold additional signaling proteins.
There are 16 human G protein subtypes from 4 families that can be involved in biased signaling.
Data
- Sequences
- 16 Human G proteins
- 317 Species orthologs
- Couplings
- 3,730 G protein couplings
- Structures
- 498 G proteins
- 298 G protein complexes
- 539 Generic residues
- Structure models
- 3,058 G protein complexes
- 245 Refined complexes
- Structure interactions
- 0 G protein interface
- Mutations
- 54 Interface mutations
Latest release
Nov. 3, 2022- New refined GPCR structures using AlphaFold
- New full-length and state-specific AlphaFold models for all human GPCRs
- New functionality for searching ligands by name, database identifier, or SMILES/InChIKey
- Updated the ligand and bioactivity pages
- Updated GPCR ligands and bioactivities with data from Guide to Pharmacology and PDSP Ki
- Updated the new Endogenous ligands browser
- Minor bug and performance fixes
All releases
Related resources
GPCRdb, GproteinDb, ArrestinDb and Biased Signaling Atlas cover related aspects of signal transduction while serving dedicated research communities and use cases. Together, they have served 5,895/51,693 users in the last month/year (Google Analytics)Publications
The G protein database, GproteinDb.Pandy-Szekeres G, Esguerra M, Hauser AS, Caroli J, Munk C, Pilger S, Keseru GM, Kooistra AJ, Gloriam DE
Nucleic acids research, 2022, 50:D518-D525