California Polytechnic State University
San Luis Obispo 1983
M.S., Cornell University, New York 1985
Ph.D., Cornell University, New York 1989
Postdoctoral, Rutgers University,
Piscataway, New Jersey 1990-1993
Postdoctoral, Schering Plough Research Institute,
Kenilworth, New Jersey 1993-1995
Our laboratory is interested in determining the
three-dimensional structures of small proteins in solution by
multidimensional multinuclear nuclear magnetic resonance (NMR)
spectroscopy. Current projects underway in the laboratory focus
on relating structure to function and specificity in the Grb7
protein family. Members of this protein family have all been
implicated in an increased occurrence of cancer. Specifically,
Grb7 expression is up-regulated in 20-30% of breast cancers and
these patients have a poor long-term survival rate. Our research
is focused on unraveling the structural basis for the propensity
of this protein family to bind only to specific up-stream and
down-stream signaling partners. Study in this field spans a wide
breadth of experimental approaches, including molecular biology,
expression, and purification of proteins of interest, knowledge
and implementation of data acquisition techniques using the NMR
spectrometer, extensive data analysis and interpretation using
available software on Unix based computers, and calculation and
refinement of three-dimensional structures derived from NOE
Solution Structure of the
Grb14-SH2 Domain and Comparison to the Structure and Backbone
Relaxation Behavior of the Grb7-SH2/erbB2 Peptide Complex.
Scharf, P.J.; Ivancic, M.; Guth, E.C.; Witney, J.; Daugherty,
M.A.; Lyons, B.A.
(Submitted to: Proteins: Structure, Function, and Bioinformatics)
Solution Structure of the Human
Grb7-SH2 Domain/erbB2 Peptide Complex and Structural Basis for
Grb7 Binding to erbB2.
Ivancic, M.; Daly, R.J.; Lyons, B.A. (2003)
J Biomol NMR, Nov;27(3):205-19.
Assignment of Backbone 1H, 13C,
and 15N Resonances of the SH2 Domain of Human Grb14.
Scharf, P.J.; Lyons B.A. (2002)
J Biomol NMR, Nov;24(3):275-6.
Assignment of Backbone 1H, 13C,
and 15N Resonances of Human Grb7-SH2 Domain in Complex with a
Phosphorylated Peptide Ligand.
Brescia, P.J.; Ivancic, M.; Lyons, B.A. (2002)
J Biomol NMR, May;23(1):77-8.
Spectral and Metal-Binding
Properties of Three Single-Point Tryptophan Mutants of Human
He, Q.Y.; Mason, A.; Lyons, B.; Tam, B.; Nguyen, V.; MacGillivray,
R.; Woodworth, R. (2001)
The Biochemistry Journal 354, 423.
Uracil Glycol Deoxynucleoside
Triphosphate is a Better Substrate for DNA Polymerase I Klenow
Fragment than Thymine Glycol Deoxynucleoside Triphosphate.
Purmal, A.A.; Bond, J.P.; Lyons, B.A.; Kow, Y.W.; & Wallace, S.S.
Chemical Shift Assignments and
Secondary Structure of the Grb2 SH2 Domain by Heteronuclear NMR
Wang, Y.S.; Frederick, A.F.; Senior, M.M.; Lyons, B.A.; Black, S.;
Kirschmeier, P.; Perkins, L.M.; & Wilson, O. (1996)
J Biomol NMR 7(2):89-98.
The Mechanism of Binding
Staphylococcal Protein A to Immunoglobin G Does Not Involve Helix
Jendeberg, L.; Tashiro, M.; Tejero, R.; Lyons, B.A.; Uhlen, M.;
Montelione, G.T.; & Nilsson, B. (1996)
An Improved Strategy for
Determining Resonance Assignments for Isotopically Enriched
Proteins and Its Application to an Engineered Domain of
Staphylococcal Protein A.
Lyons, B.A.; Tashiro, M.; Cedergren, L.; Nilsson, B.; & Montelione,
General Approach for Determining Scalar Coupling Constants in
Polypeptides and Proteins.
Montelione, G.T.; Emerson, S.D.; & Lyons, B.A. (1992)