Pär Nordlund Group
Pär Nordlund's profile page.
The main research interest of the laboratory is the structural basis for the function of proteins involved in disease processes, with a particular emphasis on cancer, inflammation and infectious diseases. The group encompasses an X-ray based structural biology unit and applies a wide range of biophysical and biochemical techniques to study protein function. The laboratory also has a track record in developing "high-throughput" technologies for solving bottlenecks in protein production, crystallization and structure analysis.
The current biological focus of the group is:
- Studies of integral membrane proteins involved in cell signalling and transport
- Studies of proteins in cancer related pathways
- Studies of Herpes proteins involved in replication and the circumvention of the human apoptosis and immune responses.
|Christian Löw||Assistant professor|
Three-dimensional structure of the free radical protein of ribonucleotide reductase.
Nature 1990 Jun;345(6276):593-8
Unusual clustering of carboxyl side chains in the core of iron-free ribonucleotide reductase.
Nature 1993 Jan;361(6409):276-8
Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane.
Nature 1993 Dec;366(6455):537-43
The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase.
Nature 1994 Aug;370(6490):575-8
A glycyl radical site in the crystal structure of a class III ribonucleotide reductase.
Science 1999 Mar;283(5407):1499-504
Crystal structure of a human mitochondrial deoxyribonucleotidase.
Nat. Struct. Biol. 2002 Oct;9(10):779-87
Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase.
Nat. Struct. Mol. Biol. 2004 Nov;11(11):1142-9
The radical site in chlamydial ribonucleotide reductase defines a new R2 subclass.
Science 2004 Jul;305(5681):245-8
Crystal structure of a divalent metal ion transporter CorA at 2.9 angstrom resolution.
Science 2006 Jul;313(5785):354-7
Structural basis for synthesis of inflammatory mediators by human leukotriene C4 synthase.
Nature 2007 Aug;448(7153):613-6
Monitoring drug target engagement in cells and tissues using the cellular thermal shift assay.
Science 2013 Jul;341(6141):84-7
Abstract at sciencemag.org
Reprint at sciencemag.org
Full Text at sciencemag.org