Pär Nordlund Group


Pär Nordlund

E-mail: Par.Nordlund@ki.se

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.

Research group

Henriette LaursenScholar
Christian LöwAssistant professor
Esben QuistgardPostdoc

Selected Publications

Three-dimensional structure of the free radical protein of ribonucleotide reductase.
Nordlund P, Sjöberg B, Eklund H
Nature 1990 Jun;345(6276):593-8

Unusual clustering of carboxyl side chains in the core of iron-free ribonucleotide reductase.
Aberg A, Nordlund P, Eklund H
Nature 1993 Jan;361(6409):276-8

Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane.
Rosenzweig A, Frederick C, Lippard S, Nordlund P
Nature 1993 Dec;366(6455):537-43

The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase.
Su X, Taddei N, Stefani M, Ramponi G, Nordlund P
Nature 1994 Aug;370(6490):575-8

A glycyl radical site in the crystal structure of a class III ribonucleotide reductase.
Logan D, Andersson J, Sjöberg B, Nordlund P
Science 1999 Mar;283(5407):1499-504

Crystal structure of a human mitochondrial deoxyribonucleotidase.
Rinaldo-Matthis A, Rampazzo C, Reichard P, Bianchi V, Nordlund P
Nat. Struct. Biol. 2002 Oct;9(10):779-87

Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase.
Larsson K, Jordan A, Eliasson R, Reichard P, Logan D, Nordlund P
Nat. Struct. Mol. Biol. 2004 Nov;11(11):1142-9

The radical site in chlamydial ribonucleotide reductase defines a new R2 subclass.
Högbom M, Stenmark P, Voevodskaya N, McClarty G, Gräslund A, Nordlund P
Science 2004 Jul;305(5681):245-8

Crystal structure of a divalent metal ion transporter CorA at 2.9 angstrom resolution.
Eshaghi S, Niegowski D, Kohl A, Martinez Molina D, Lesley S, Nordlund P
Science 2006 Jul;313(5785):354-7

Structural basis for synthesis of inflammatory mediators by human leukotriene C4 synthase.
Martinez Molina D, Wetterholm A, Kohl A, McCarthy A, Niegowski D, Ohlson E, et al
Nature 2007 Aug;448(7153):613-6

Monitoring drug target engagement in cells and tissues using the cellular thermal shift assay.
Martinez Molina D, Jafari R, Ignatushchenko M, Seki T, Larsson E, Dan C, et al
Science 2013 Jul;341(6141):84-7
Abstract at sciencemag.org
Reprint at sciencemag.org
Full Text at sciencemag.org