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| Peter J Winn, European Molecular Biology Laboratory |
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Peter Winn is an NIH postdoctoral fellow based at EMBL, Heidelberg. His interests are in protein structure-function analysis from individual proteins through to protein complexes. Currently, his research focuses on structure function in the cytrochromes P450, and their regulation by ubiquitination, as well as how higher level protein organisation is related to cellular function.
Selected publications.
1. P. J. Winn, T. L. Religa, J. N. D. Battey, A. Banerjee, R. C. Wade. A comparative analysis of the interaction properties of the E2 ubiquitin conjugating enzymes and related proteins. Structure In Press
2. P. J. Winn, S. K. Luedemann, R. Gauges, V. Lounnas and R. C. Wade. Comparison of the dynamics of substrate access channels in three cytochrome P450s reveals different opening mechanisms and a new functional role for a buried arginine. PNAS (USA), 2002, 99(8), 5361-5366.
3. P. J. Winn, G. G. Ferenczy, C. A. Reynolds. Towards improved force fields III. Polarization through modified atomic charges. J. Comp. Chem, 1999, 20(7), 704 - 712.
4. P. J. Winn, G. G. Ferenczy, C. A. Reynolds. Towards improved force fields. I. Multipole-derived atomic charges. J. Phys. Chem., 1997, 101(30), 5437-5445.
5. P. R. Gouldson, P. J. Winn, C. A. Reynolds. A molecular dynamics approach to receptor mapping: application to the 5HT3 and beta 2-adrenergic receptors. J. Med. Chem., 1995, 38(20), 4080-4086.
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Determinants of Functionality in the Ubiquitin Conjugating Enzyme Family
Peter J Winn, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg Germany
The E2 enzymes are key enzymes in the ubiquitin and ubiquitin-like protein ligation pathways. Ubiquitination is a post-translational modification of proteins that is important for proteasomal degradation, DNA repair and many other fundamental cellular processes (VanDemark et al., 2001, Weissman, 2001). Disruption of the ubiquitin system has been implicated in a large number of diseases, including many forms of cancer and neurodegenerative diseases (Reboud-Ravaux, 2002).
To understand the different E2 enzymes, we analysed 190 protein sequences and 211 structures and electrostatic potentials. Key findings include: An N-terminal sequence motif that is highly conserved in all E2s except for Cdc34 orthologs is important for the stabilisation of the L7 loop and is likely to be involved in E1 binding. All the E2s known to ubiquitinate histones have a negative potential. The ScUbc1 orthologs are defined by a C-terminal UBA domain. ScUbc11p has a different electrostatic potential from E2-Cp and other proteins with which it has high sequence similarity but different functionality. The NCUBE family have a positive electrostatic potential, although its form is different from that of the E2 that conjugate SUMO (a ubiquitin likeprotein). The specificities of only the ScUbc4/Ubc5 and ScUbc1p orthologs are reflected in their L4 and L7 loops.
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