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Research Interests

The main focus of my group is the application of Nuclear Magnetic Resonance (NMR) spectroscopy, molecular biological, biochemical and biophysical techniques to characterize the structure, dynamics and molecular interactions of multidomain proteins involved in normal cell regulation and cancer metastasis. Regulatory processes within the cell are mediated via molecular interactions that lead to the formation of macromolecular complexes. The molecular interactions within these complexes are modulated through different domains within individual proteins that have the capacity to interact with other proteins and nucleic acids. The study of the structural details of protein-protein, protein-RNA and protein-DNA interactions is necessary to understand the function of the individual components of the complexes that are involved in transcriptional, post-transcriptional, translational and post-translational regulation.

Selected Publications

G. C. Pérez-Alvarado, M. Martínez-Yamout, M. M. Allen, R. Grosschedl, H. J. Dyson & P. E. Wright.  Structure of the nuclear factor ALY: Insights into post-transcriptional regulatory and mRNA nuclear export processes.  Biochemistry 42 (24), 7348-7357 (2003).

G. C. Pérez-Alvarado, A. Munnerlyn, H.J. Dyson, R. Grosschedl & P.E. Wright.  Identification of the residues involved in DNA binding by the mouse PEBP2a protein.  FEBS Letters  470, 125-130 (2000).

I. Radhakrishnan, G. C. Pérez-Alvarado, D. Parker, H. J. Dyson, M. R. Montminy & P. E. Wright.  Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions.  Cell  91, 741-752 (1997).

G. C. Pérez-Alvarado, J. L. Kosa, H. A. Louis, M. C. Beckerle, D. R. Winge & M. F. Summers. Structure of the cysteine-rich intestinal protein, CRIP. J. Mol. Biol. 257, 153-174 (1996).

G. C. Pérez-Alvarado, C. Miles, J. W. Michelsen, H. A. Louis, D. R. Winge, M. C. Beckerle & M. F. Summers. Structure of the C-terminal LIM domain from the cysteine rich protein CRP. Nat. Struct. Biol. 1, 388-398 (1994).