Center for Membrane Protein Research
Mission: The long-term goal of the Center is to advance our knowledge of the structure and function of membrane proteins in health and disease. The Center brings together a group of TTUHSC and TTU investigators interested in the broad field of membrane-protein research.Rationale: After completion of the human genome sequence, biomedical research has evolved into a combination of genomics, proteomics, and functional genomics. To a great extent, biomedical research in this century will be focused on prototypical proteins and protein families, including the determination of their structures, normal function, and their roles in human disease. From this knowledge will emanate rational design of new pharmacological agents that will open novel therapeutic approaches.
About 30% of the genes included in the human genome encode membrane proteins. These proteins participate in a myriad of normal and abnormal cell functions, including: 1) transport of ions, water and small solutes; 2) signaling processes; 3) metabolism and detoxification; 4) programmed cell death and necrosis; 5) entry of pathogens into cells, and 6) cellular structural integrity. If the promise of modern proteomics is to be fully realized, greater attention must be paid to the structures of these proteins and how they relate to normal and abnormal function. Crystallization is the method of choice for generating high-resolution structural models. However, membrane proteins have both hydrophobic and hydrophilic surfaces, a duality that makes them more difficult to crystallize than water-soluble proteins. It follows that relatively few structures of membrane proteins have been solved at the level of atomic resolution. In addition, high-resolution structures are important but not sufficient to understand how membrane proteins (and soluble proteins as well) function. To assess function, it is necessary to carry out biochemical and biophysical studies that are informed by structural knowledge, but explore questions of molecular mechanism, protein-protein interactions, and regulation.
Membrane Protein Core Laboratory (MPCL)
Annual Meeting 2009 (May 2009)
"Overview of CMPR" Presentation (Dr. Blanton, July 2009)
Membership:
- Guillermo Altenberg, M.D., Ph.D., Associate Professor
Structure, function and regulation of normal gap-junctional proteins and mutants that cause heart disease and deafness.
(806) 743-2531, G.Altenberg@ttuhsc.edu
- Pablo Artigas, Ph.D., Assistant Professor
Structure based functional studies of Na/K ATPase and bilayer regulation of membrane protein function.
(806) 743-3170, Pablo.Artigas@ttuhsc.edu
- Michael P. Blanton, Ph.D., Associate Professor
Structural analysis of ligand gated channels.
(806) 743-2425, Michael.Blanton@ttuhsc.edu
- Luis Cuello, Ph.D., Assistant Professor
Structure-function studies of voltage-gated K+ channels.
(806) 743-2525, Luis.Cuello@ttuhsc.edu
- Joe A. Fralick, Ph.D., Professor
Transport physiology of bacteria.
(806) 743-2555, Joe.Fralick@ttuhsc.edu
- Lan Guan, M.D., Ph.D., Assistant Professor
High-resolution structure modeling of solute transporters.
(806) 743-3102, Lan.Guan@ttuhsc.edu
- Juyang Huang, Ph.D., Associate Professor
The role of cholesterol in determining the physical, chemical and functional properties of biomembranes.
(806) 742-4780, Juyang.Huang@ttu.edu
- Michaela Jansen, Ph.D., Assistant Professor
Structure and function studies of ligand-gated ion channels and transporters.
(806) 743-4059, Michaela.Jansen@ttuhsc.edu
- Jose Perez-Zoghbi, Ph.D., Assistant Professor
The cellular mechanisms of epithelium-smooth muscle communication in the lung.
(806) 743-2522, Jf.Perez@ttuhsc.edu
- Thomas A. Pressley, Ph.D., Professor
Function and regulation of the sodium-potassium pump and similar ion transporters.
(806) 743-4056, Thomas.Pressley@ttuhsc.edu
- Luis Reuss, M.D., Professor and Director
Ion and water transport mechanisms; structure and function of gap-junction channels and hemichannels.
(806) 743-2627, Luis.Reuss@ttuhsc.edu
- R. Bryan Sutton, Ph.D., Associate Professor
X-ray crystallography of peripheral membrane associating C2 domains in synaptotagmin and human dysferlin.
(806) 743-4058, Roger.B.Sutton@ttuhsc.edu
- Ina Urbatsch, Ph.D., Assistant Professor
Structure-function relationships in the multidrug-resistance proteins.
(806) 743-2700, Ina.Urbatsch@ttuhsc.edu
- Joachim Weber, Ph.D., Assistant Professor
Enzymatic mechanism of ATP synthesis by the ATP synthase.
(806) 742-1297, Joachim.Weber@ttuhsc.edu