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Department of Biochemistry and Molecular Biology

Houston, Texas

Images from biochemistry and molecular biology research
Verna and Marrs McLean Department of Biochemistry and Molecular Biology
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Florante A. Quiocho, Ph.D.

Quiocho photo

Charles C. Bell Professor, Structural Biology

Professor, Dept. of Biochemistry & Molecular Biology

Professor, Dept. of Molecular Physiology & Biophysics

faq@bcm.edu

Education

  • Ph.D., Biochemistry, 1966, Yale University

Structural Biophysics and Biology: X-Ray Crystallography of Proteins

Three-dimensional structures of biological macromolecules lie at the very core of understanding, at the atomic level, biological and biochemical processes. Our research interest is centered on the study of the three-dimensional structure and function of proteins and enzymes at atomic resolution. Although x-ray crystallography is the primary experimental approach to achieve this goal, other correlative studies employing biochemical, physical-chemical, and recombinant DNA techniques are also being pursued. The proteins under investigation cover the areas of signal transduction and cellular regulation, active transport, ligand and drug molecular recognition and vesicular trafficking and membrane fusion.

Sec15 is a component of the exocyst complex involved in vesicle transport and localization. It recognizes vesicles associated with Rab GTPases. The C-terminal helical domain of Drosophila Sec15 (left, x-ray structure) interacts with Rab11 in a GTP-dependent manner, co-localizes with this Rab GTPase in specialized structures within the fly eye called rhabdomeres (right, cover), and is important for rhabdomere morphology.
Sec15 is a component of the exocyst complex involved in vesicle transport and localization. It recognizes vesicles associated with Rab GTPases. The C-terminal helical domain of Drosophila Sec15 (left, x-ray structure) interacts with Rab11 in a GTP-dependent manner, co-localizes with this Rab GTPase in specialized structures within the fly eye called rhabdomeres (right, cover), and is important for rhabdomere morphology. Wu, S., Mehta, S.Q., Pichaud, F., Bellen, H.J. & Quiocho, F.A. Nature Struct. Molec. Biol. 12, 879-885 (2005)

View Publications by Dr. Quiocho.

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