Welcome to the GPCRDB

The GPCRDB is a molecular-class information system that collects, combines, validates and stores large amounts of heterogenous data on G protein-coupled receptors (GPCRs). The GPCRDB contains data on sequences, ligand binding constants and mutations. In addition, many different types of computationally derived data are stored such as multiple sequence alignments and homology models. The GPCRDB is designed to be a data storage medium, as well as a tool to aid biomedical scientists with answering questions by offering a single point of access to many types of data that are integrated and visualized in a user-friendly way. Although most parts of the GPCRDB are self-explanatory, if you have not used this resource before we advice you to take a look at the usage page.

We advice you to take a look at the:
- updates page to see what has changed and what is new
- usage page to make sure you will quickly find your way

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NEW! The next generation of GPCRDB

A new GPCRDB release is available HERE. The new interface focuses on usability for GPCR researchers from all disciplines, and features a number of new tools and diagrams:

  • Crystal structure browser: Finds the most relevant structure by filtering for manually curated ligand and receptor data, and target-template sequence similarity measures (Isberg et al., Nucleic Acids Res. 2014;42:D422-5.).
  • Structural tools: Superposition of multiple uploaded GPCR structures (pdb format), on the overall structure or sub-site residues, e.g. lining a common ligand-binding pocket, in the transmembrane domain.
  • Receptor residue diagrams: Snake-plots and helix box diagrams are used to visualise the topological position of for example receptor mutants, and can swiftly be custom-coloured and downloaded for publication/presentation.
  • Receptor mutants: Researchers can now voluntarily contribute published mutagenesis data to increase its dissemination and compare it to the previously reported. Data quality is ensured by the use of a standardised excel file, and internal approval.
  • Structure-based sequence alignments: The first to take into account structural distortions, bulges and constrictions, in the transmembrane helices so that spatially equivalent residues aligned in a structural comparison are also the ones aligned in sequence (by gapping TM helices).
  • GPCR residue numbers: GPCRDB numbers can be assigned to sequences, structures or pdf articles (Isberg et al., Trends Pharmacol Sci. 2015;36(1):22-31.).
  • Receptor similarities: Find the most similar receptor by matching the GPCRDB reference sequence alignments, swiftly depict relationships in phylogenetic trees, or make a sequence motif search to profile receptors with e.g. a common binding site.
  • Receptor cross-references: To the IUPHAR GuideToPharmacology database.

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GPCR-specific PDF reader

We are proud to release the GPCR-specific PDF reader, built using the best parts of the GPCRDB and the Utopia Documents PDF reader. The reader allows you to enrich your scientific literature with information and knowledge from the GPCRDB. More details can be found here. Try it!

The informal collaboration of GPCR databases

These include GPCRDB at the CMBI, the Netherlands (formerly at the EMBL), tinyGRAP Mutant Database at the CMBI (formerly at Tromso, Norway), The GPCR Oligomerization Knowledge Base (GPCR-OKB) at the Weill Medical College of Cornell University, Swiss-Prot and the GPCR Natural Variants Database (NaVa).

Current version: 2013.09.26