GPCRdb in 2021: integrating GPCR sequence, structure and function
Open accessAbstract
G protein-coupled receptors (GPCRs) form both the largest family of membrane proteins and drug targets, mediating the action of one-third of medicines. The GPCR database, GPCRdb serves >4 000 researchers every month and offers reference data, analysis of own or literature data, experiment design and dissemination of published datasets. Here, we describe new and updated GPCRdb resources with a particular focus on integration of sequence, structure and function. GPCRdb contains all human non-olfactory GPCRs (and >27 000 orthologs), G-proteins and arrestins. It includes over 2 000 drug and in-trial agents and nearly 200 000 ligands with activity and availability data. GPCRdb annotates all published GPCR structures (updated monthly), which are also offered in a refined version (with re-modeled missing/distorted regions and reverted mutations) and provides structure models of all human non-olfactory receptors in inactive, intermediate and active states. Mutagenesis data in the GPCRdb spans natural genetic variants, GPCR-G protein interfaces, ligand sites and thermostabilising mutations. A new sequence signature tool for identification of functional residue determinants has been added and two data driven tools to design ligand site mutations and constructs for structure determination have been updated extending their coverage of receptors and modifications. The GPCRdb is available at https://gpcrdb.org.
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RoseTTAFold has been evaluated since May 15th, 2021 on CAMEO; over the 69 medium and hard targets released during this time, it outperformed all other servers evaluated including Robetta, IntFold6-TS, BestSingleTemplate, and SWISS-MODEL.
“RoseTTAFold has been evaluated since May 15th, 2021 on CAMEO; over the 69 medium and hard targets released during this time (May 15th, 2021 ~ June 19th, 2021), it outperformed all other servers evaluated in the experiment including Robetta (3), IntFold6-TS (8), BestSingleTemplate (9), and SWISS-MODEL (10) (Fig. 1C).”
From Accurate prediction of protein structures and interactions using a 3-track network (2021) · cites this paper as [8]
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- Authors
- Kooistra, A. J., Mordalski, S., Pándy-Szekeres, G., Esguerra, M., Mamyrbekov, A., Munk, C., Keserű, G. M., & Gloriam, D. E.
- Affiliations
- University of Copenhagen (DK)
- Department of Drug Design and Pharmacology, University of Copenhagen, Universitetsparken 2, 2100 Copenhagen, Denmark
- HUN-REN Research Centre for Natural Sciences (HU)
- Corresponding author
- Kooistra, Albert J
- Gloriam, David E
- ORCID
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2020-12-03
- Volume
- 49
- Issue
- D1
- Pages
- D335-D343
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC7778909
- OpenAlex
- W3110608978
- Cited by
- 351
- References
- 36
- Citations by year
- 2026: 25 · 2025: 39 · 2024: 56 · 2023: 67 · 2022: 117 · 2021: 44 · 2020: 2
- FWCI
- 18.88
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Nucleic Acids Research (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, cc-by)
- Funders
- Lundbeck Foundation (R218-2016-1266, R163-2013-16327)
- Horizon 2020 (765657)
- Independent Research Fund Denmark (8021-00173B)
- Novo Nordisk Foundation (NNF18OC0031226)
- Alfred Benzon Foundation (ABF-0-0-312)
- Polish National Science Center (2015/18/M/NZ2/00423)
- National Research, Development and Innovation Office, Hungary (2017-1.2.1-NKP-2017-00002)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Physical Sciences › Computer Science › Computational Theory and Mathematics › Computational Drug Discovery Methods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- G protein-coupled receptors, GPCRdb, G proteins, arrestin, GPCR structure, ligand binding sites, mutagenesis, sequence signatures, structural model, therapeutic target
- MeSH terms
- Amino Acid Sequence, Pharmaceutical Preparations, Ligands, Phylogeny, Signal Transduction, Sequence Alignment, Conserved Sequence, GTP-Binding Proteins, Databases, Protein, Receptors, G-Protein-Coupled
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