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FRISC: The Faculty Research Interests Science Comparator |
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Professor of Biochemistry
Investigator, Howard Huges Medical Institute
Biological Chemistry
Molecular Biophysics
Office: (214) 648-5089
FAX: (214) 648-5095
Email: Johann.Deisenhofer@email.swmed.edu
Home Page: Deisenhofer Lab
Crystallography is the predominant method by which
structural information at atomic resolution on large (> 40 kD) protein molecules can be
obtained. Such information is key to understanding the function of proteins, and a basis
for the design of mutants and drugs.
We have crystallized and determined the 3-D structures of
water-soluble proteins and integral membrane proteins. Main criteria for selection of
proteins are their biological significance, unusual amino acid sequences, and involvement
in electron transfer or energy transfer processes. Current projects include: Cytochrome
bc1 complexes from bovine heart mitochondria and from a photosynthetic purple bacterium,
the active iron transporter FepA from the outer membrane of E. coli, the extracellular
domains of the LDL receptor, the murine MHC class I molecule H2-M3 loaded with different
peptides, a T-cell receptor Valpha dimer, the light activated DNA repair enzyme photolyase
in a complex with a substrate, photolyase-related blue light photorecptors, proteins from
the bacterial UvrABC DNA excision repair system, the neural proteins synapsin and neurexin
1, and the mitochondrial processing peptidase from yeast.
Please, visit our lab home page for more
information.
Selected Publications:
Buchanan, S.K., Smith, B.S., Venkatramani, L., Xia, D.,
Esser, L., Palnitkar, M., Chakraborty, R., Van der Helm, D. and Deisenhofer, J. (1999)
Crystal structure of the outer membrane active transporter FepA from Escherichia coli. Nature
Structural Biology , 6, 56-63.
Esser, L., Wang, C.-R., Hosaka, M., Smagula, C.S.,
Südhof, T.C. and Deisenhofer, J. (1998) Synapsin I is structurally similar to
ATP-utilizing enzymes. EMBO Journal , 17, 977-984.
Kim, H., Xia, D., Yu, C.-A., Xia, J.-Z., Kachurin, A.M.,
Zhang, L., Yu, L. and Deisenhofer, J. (1998) Inhibitor binding changes domain mobility in
the iron sulfur protein of the mitochondrial bc1 complex from bovine heart. Proc. Natl.
Acad. Sci. USA , 95, 8026-8033.
Xia, D., Yu, C.A., Kim, H., Xian, J.Z., Kachurin, A.M.,
Zhang, L., Yu, L. and Deisenhofer, J. (1997) Crystal structure of the cytochrome bc1
complex from bovine heart mitochondria. Science , 277, 60-66.
Hunt, J.F., Van der Vies, S.M., Henry, L. and Deisenhofer,
J. (1997) Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31
expand the size of the Anfinsen cage. Cell , 90, 361-371.
Hunt, J.F., Weaver, A.J., Landry, S.J., Gierasch, L.M. and
Deisenhofer, J. (1996) The crystal structure of the GroES co-chaperonin at 2.8 Å
resolution. Nature , 379, 37-45.
Wang, C.-R., Castaño, A.R., Peterson, P.A., Slaughter,
C.A., Fischer Lindahl, K. and Deisenhofer, J. (1995) Nonclassical binding of formylated
peptide in crystal structure of the MHC Class Ib molecule H2-M3. Cell , 82, 655-664.
Park, H.-W., Kim, S.-T., Sancar, A. and Deisenhofer, J.
(1995) Crystal structure of DNA photolyase from Escherichia coli. Science , 268,
1866 1872.
Kobe, B. and Deisenhofer, J. (1995) A structural basis of
the interactions between leucine-rich repeats and protein ligands. Nature , 374,
183-186.
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Last updated: 17 Nov 2000
Extraction Method: Expand using Medical Synonyms-
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