Brian Kobilka

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Brian Kobilka in 2007
3D structural model of the β 2 -adrenoceptor with the inverse agonist carazolol

Brian Kent Kobilka (born May 30, 1955 in Little Falls , Minnesota ) is an American biochemist . On October 10, 2012, the professor at the Stanford University School of Medicine was awarded the Nobel Prize in Chemistry together with Robert Lefkowitz “for their studies on G-protein-coupled receptors ”.

Life and Scientific Work

Brian K. Kobilka's father and grandfather were bakers by trade. Kobilka studied biology and chemistry at the University of Minnesota Duluth and graduated from the School of Medicine at Yale University after his bachelor's degree . After further training in internal medicine at Barnes Hospital, Washington University in St. Louis , he worked as a postdoc with Robert Lefkowitz at Duke University . Since then, he has paid special attention to the β 2 -adrenoceptor , a protein from the group of G-protein-coupled receptors that is involved in the action of the hormone adrenaline . During his time at Duke University, he and colleagues succeeded in cloning a ligand-gated G-protein-coupled receptor for the first time . This not only represented a milestone in research into the pharmacologically most important group of proteins, but also opened up new possibilities for drug research. In 1994 he received the John J. Abel Award in Pharmacology. In 2007 and the following years, Brian Kobilka published a series of papers on the spatial structure and three-dimensional functioning of G-protein-coupled receptors, a class of proteins that until then was considered to be almost inaccessible to structural analysis. In 2010 he received the ASPET- Julius Axelrod Award. In 2011 he was accepted by the National Academy of Sciences . In 2012 he was awarded the Nobel Prize in Chemistry. In 2013 he became an honorary member of the Royal Irish Academy . In 2015 he was elected to the American Academy of Arts and Sciences . Kobilka Einstein has been a Visiting Fellow at the Berlin Institute of Health since 2016 .

He met his wife Tong Sun Thian at the University of Minnesota. You have two children.

Publications (selection)

literature

Web links

Commons : Brian Kobilka  - collection of images, videos and audio files

Individual evidence

  1. Richard AF Dixon, Brian K. Kobilka et al .: Cloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsin. In: Nature , Vol. 321, No. 6065, 1986, pp. 75-79, doi: 10.1038 / 321075a0 , PMID 3010132 .
  2. Wadim Tscheresow, Daniel M. Rosenbaum et al .: High-Resolution Crystal Structure of an Engineered Human β 2 -Adrenergic G Protein – Coupled Receptor. In: Science , Volume 318, No. 5854, 2007, pp. 1258-1265, doi: 10.1126 / science.1150577 , PMID 17962520 .
  3. ^ Daniel M. Rosenbaum, Wadim Tscheresow et al .: GPCR Engineering Yields High-Resolution Structural Insights into β-Adrenergic Receptor Function. In: Science Volume 318, No. 5854, 2007, pp. 1266-1273, doi: 10.1126 / science.1150609 , PMID 17962519 .
  4. Søren GF Rasmussen, Choi Hee-jung et al .: Crystal structure of the human beta2 adrenergic G-protein-coupled receptor. In: Nature , Volume 450, No. 7168, 2007, pp. 383-387, doi: 10.1038 / nature06325 , PMID 17952055 .
  5. Michael P. Bokoch, Zou Yaozhong et al .: Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor. In: Nature , Volume 463, No. 7277, 2010, pp. 108-112, doi: 10.1038 / nature08650 , PMID 20054398 .
  6. Chung Ka Young, Søren GF Rasmussen et al .: Conformational changes in the G protein Gs induced by the β2 adrenergic receptor. In: Nature , Volume 477, No. 7366, 2011, pp. 611-615, doi: 10.1038 / nature10488 , PMID 21956331 .
  7. 2010 ASPET Award Winners at the American Society for Pharmacology and Experimental Therapeutics , accessed February 20, 2016.
  8. ^ Members: Brian Kent Kobilka. Royal Irish Academy, accessed May 9, 2019 .
  9. ^ Brian Kobilka . In: Einstein BIH Visiting Fellows. Einstein Foundation Berlin, accessed on May 23, 2018.
  10. Lizzie Buchen: Cell signaling: It's all about the structure. In: Nature , Volume 476, No. 7361, 2011, pp. 387-390, doi: 10.1038 / 476387a .