5 February 2019
GPCRs are cell-surface receptors, and they are a very important drug target: 34% of all drugs approved in the US act on GPCRs. For rational drug design, structures of the receptors are needed. GPCRs are difficult to crystallize, because they are very flexible and hydrophobic. In the past decade, much progress has been made in measuring GPCR structures, but there is no structure for the majority of receptors (87%) and there is a lack in knowledge about the intermediate and active states of GPCRs. The GPCRdb now offers a tool that helps to design mutations, choose fusion proteins and choose experimental conditions in order to successfully crystallize a receptor.
The GPCRdb contains data, diagrams and web tools for G protein-coupled receptors (GPCRs). This resource was founded by professor Gert Vriend, theme Nanomedicine, and is now maintained and expanded by the group of David Gloriam in Copenhagen.
The most recent addition to the GPCRdb is a web tool to make the design of crystal constructs easier. CMBI Master's student Janne Bibbe (photo) was part of this project, and is now co-author of the paper "An online resource for GPCR structure determination and analysis" in Nature Methods.GPCRs are cell-surface receptors, and they are a very important drug target: 34% of all drugs approved in the US act on GPCRs. For rational drug design, structures of the receptors are needed. GPCRs are difficult to crystallize, because they are very flexible and hydrophobic. In the past decade, much progress has been made in measuring GPCR structures, but there is no structure for the majority of receptors (87%) and there is a lack in knowledge about the intermediate and active states of GPCRs. The GPCRdb now offers a tool that helps to design mutations, choose fusion proteins and choose experimental conditions in order to successfully crystallize a receptor.