News

Nobel Prize winner presents on cholesterol transport



6 September 2010

Hear Professor Johann Deisenhofer, winner of the Nobel Prize in Chemistry 1988, present on cholesterol transport at a special seminar at the University of Sydney on 15 September 2010.

Professor Johann Deisenhofer, winner of the Nobel Prize in Chemistry 1988, present on cholesterol transport at a special seminar at the University of Sydney on 15 September 2010.
Professor Johann Deisenhofer, winner of the Nobel Prize in Chemistry 1988, present on cholesterol transport at a special seminar at the University of Sydney on 15 September 2010.

Professor Johann Deisenhofer, from the University of Texas Southwestern Medical Center, Dallas, Texas, USA, will present on structural studies of cholesterol transport.

The free talk will be held at 1pm in Lecture Theatre 104 in the New Law School Building, Eastern Avenue, University of Sydney.

Cholesterol is essential for mammals - it is produced internally or taken up with the diet and transported in the blood stream in the form of lipoproteins, with low density lipoprotein (LDL) being most abundant.

LDL is bound at cell surfaces by receptors and internalised. Inside cells, LDL particles are released from the receptors, degraded in lysosomes, and cholesterol is transported by specific binding proteins to its destinations.

Professor Deisenhofer will describe four studies that he has published on structural aspects of cholesterol transport:

  • Electron microscopy of low density lipoprotein (LDL) with and without bound LDL receptor protein shows size, shape and internal structure of typical LDL particles.
  • The crystal structure of the extracellular portion of human LDL receptor at pH 5.3 illustrates the domain organisation of the receptor, and suggests possible mechanisms for LDL release at low pH. The recently discovered protein PCSK9 binds to the LDL receptor and appears to regulate the degradation of the receptors.
  • A crystal structure of the complex of PCSK9 with a fragment of the LDL receptor defines the binding interface and could lead to the development of new cholesterol-lowering drugs. Mutations in the proteins NPC1 and NPC2 can cause Niemann-Pick disease by slowing down or preventing the transport of cholesterol out of lysosomes.
  • The crystal structure of the N-terminal domain of NPC1 with and without bound cholesterol sheds light on the intra-lysosomal cholesterol transport pathway.

Although Professor Deisenhofer has focussed on the structure of cholesterol in his recent work, he won the Nobel Prize in Chemistry in 1988, along with colleagues Robert Huber and Hartmut Michel, for the determination of the three-dimensional structure of the photosynthetic reaction centre molecule from Rhodopseudomonas viridis and refined the model to a 2.3 Angstrom resolution.

All are welcome to attend the free talk on 15 September 2010.

Date: Wednesday 15 September 2010
Time: 1:00pm
Cost: Free
Location: Lecture Theatre 104 in the New Law School Building, Eastern Avenue, University of Sydney.


Contact: Katynna Gill

Phone: 02 9351 6997

Email: 26130e4d0258114d051334550b3e31301630355a530601492a31