Fletterick, Robert

How would substrate preference be changed if the glycine residues in trypsin at positions 216 and 226 were changed to alanine rather than to the more bulky valine and threonine groups that are present in elastase This question was addressed by the groups of Charles Cralk, William Rutter, and Robert Fletterick in San Francisco, who have made and studied three such trypsin mutants one in which Ala is substituted for Gly at 216, one in which the same substitution is made at Gly 226, and a third containing both substitutions. 

The following, in alphabetical order, have reviewed one or more chapters, correcting our errors of fact or interpretation and helping to ensure they have the appropriate balance and emphasis Tom Alber (University of California, Berkeley), Tom Blundell (Cambridge University, UK), Stephen Burley (Rockefeller University), Charles Craik (University of California, San Francisco), Ken Dill (University of California, San Francisco), Chris Dobson (Oxford University, UK), Anthony Fink (Unversity of California, Santa Cruz), Robert Fletterick (University of California, San Francisco), Richard Henderson (LMB, Cambridge, UK), Werner Kiihlbrandt (MPI, Frankfurt), David Parry (Massey University, New Zealand), Greg Petsko (Brandeis University), and David Trentham (NIMR, London, UK). 

We thank our colleagues for their valuable contribution to this research fiber diffraction— Jeremy Bond, Sean Deverin, Dr. Leonid Shinchuk, and Dr. Deepak Sharma prions—Drs. Jack Nguyen, Michael Baldwin, Haydn Ball, Robert Fletterick, Fred Cohen, Stanley Prusiner, and Mario Salmona polyalanine—Drs. Sylvie Blondelle and Natalia Reixach and polyglutamine— Dr. Ron Wetzel. We also thank Dr. Andrew Bohm (Department of Biochemistry, Tufts University) for graciously granting us access to their X-ray diffraction facility. 

Louise Johnson and her coworkers have determined the crystal structures of T and the R forms of muscle phosphorylase b and the R form of phosphorylase a. In parallel with this work, Robert Fletterick and coworkers determined the structure of the T form of muscle phosphorylase a. The crystal structures provide an incisive look at the structural changes that accompany the transitions from the T to the R conformation and from the nonphosphorylated form of the enzyme to the phosphorylated form. 

Robert Fletterick and Mark Zoller, Current Communications in Molecular Biology Computer Graphics and Molecular Modeling, Cold Spring Harbor Laboratory, Cold Spring, NY, 1986. 

Robert J. Fletterick Departments of Biochemistry and Biophysics and Pharmaceutical Chemistry... 

The phosphorylated and unphosphorylated forms of glycogen phosphorylase have markedly different conformations, as shown by high-resolution X-ray crystallography, carried out by Louise Johnson and David Barford, in Oxford and by Robert Fletterick and Steven Sprang in San Francisco. The structures provide an explanation for the low activity of the unphosphorylated enzyme b and the high activity of the phosphorylated enzyme a (Plate 14). 

R J. Fletterick- Glyogenphosphorylase Plasticity and specificity in ligand binding. Proc Robert A. WUch Found Corf Chem Res, 27, 173-220,1992. 

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