The Wuthrich Laboratory

Pedro Serrano, PhD.

Staff Scientist

serrano@scripps.edu
phone: +1 858 784 8356
fax: +1 858 784 8014

Research Interests

As a member of the Prof. Wüthrich’s group and the Joint Center for Structural Genomics (JCSG) my research focuses primarily on the structural and functional characterization of proteins with unknown function.

Protein targets are selected from the continuously-growing genomic pool and include sequences found in all kingdoms of life. NMR structures lead to protein functional annotation and provide an unprecedented framework to understand biological processes, which will significantly impact human health and basic biological research.

A highly automated pipeline for protein production, protein solution screening and structure determination allow us to efficiently tackle a large number of potential targets, and includes NMR experiments to study ligand binding, protein dynamics and oligomeric state in solution. 

Curriculum Vitae

1999 University degree (Chemistry), Universitat de Barcelona, Spain.

2002 Diploma Master (Organic Chemistry), Universitat de Barcelona, Spain.

2004 Ph.D (Organic Chemistry), Research Unit of BioActive Molecules ( RUBAM ), IIQAB, Barcelona, Spain.

2005 Research Associate, The Scripps Research Institute, La Jolla, CA, USA.

2010 Staff Scientist, The Scripps Research Institute, La Jolla, CA, USA

Publications

1. Atia-tul-Wahab,* P. Serrano,* M. Geralt, and K. Wüthrich. NMR structure of the Bordetella bronchiseptica protein NP_888769.1 establishes a new phage-related protein family PF13554. Protein Science. 2011.

2. Orcajo, A., Ortega-Gutierrez, S., Serrano, P., Torrecillas, I. Wüthrich, K. Campillo, M., Pardo, L., Viso, A., Benhamu, B., Lopez-Rodríguez, M. J. Med. Chem. 2011, 54 (4), 1096-100. Development of Non-peptide Ligands of Growth Factor Receptor-bound Protein 2-Src Homology 2 Domain Using Molecular Modeling and NMR Spectroscopy.

3. P. Serrano*, B. Pedrini*, M. Geralt, K. Jaudzems, R. Horst, T. Herrmann, M-A. Elsliger, I. A. Wilson and K. Wüthrich, Acta Cryst. F. 2010, F66, 1393-1405. Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites.

4. J. A. Vila, P. Serrano, K. Wüthrich, H. A. Scheraga. J. Biomol. NMR. 2010, 40 (1), 23-30. Sequential nearest-neighbor effects on computed (13)C (alpha) chemical shifts.

5. B. Mohanty*, P. Serrano*, B. Pedrini, K. Jaudzems, M. Geralt,. R. Horst, T. Herrmann, M-A. Elsliger, I. A. Wilson and K. Wüthrich, Acta Cryst. F. 2010, F66, 1381-1392. Comparison of NMR and crystal structures for the proteins TM1112 and TM1367.

6. K. Jaudzems, M. Geralt, P. Serrano, B. Mohanty, R. Horst, B. Pedrini, M-A. Elsliger, I. A. Wilson, K. Wüthrich. Acta Cryst. F. 2010, F66, 1367-1380. NMR structure of the protein NP_247299.1: Comparison with the crystal structure.

7. P. Stanczak, R. Horst, P. Serrano, K. Wüthrich. J. Am. Chem. Soc. 2009, 131 (51), 18450–18456. NMR Characterization of Membrane Protein−Detergent Micelle Solutions by Use of Microcoil Equipment.

8. P. Serrano, M. A. Johnson, A. Chatterjee, Neuman, B., J. S. Joseph, M. J. Buchmeier, P. Kuhn, K. Wüthrich. J Virol. 2009, 83 (24), 12998 – 3008. NMR Structure of the Nucleic Acid-Binding Domain of the SARS Coronavirus Nonstructural Protein 3.

9. Chatterjee, A., M. A. Johnson, P. Serrano, B. Pedrini, J. S. Joseph, B. W. Neuman, K. Saikatendu, M. J. Buchmeier, P. Kuhn, and K. Wuthrich. J Virol. 2009, 83 (4), 1823–36. Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain fold.

10. Neuman, B.W., Joseph, J.S., Saikatendu, K.S., Serrano, P., Chatterjee, A., Johnson, M.A., Liao, L., Klaus, J.P., Yates, J.R., Wüthrich, K., Stevens, R., Buchmeier, M.J. and Kuhn, P. J.Virol. 2008, 82, 5279–5294. Proteomics analysis unravels the functional repertoire of Coronavirus nonstructural proten 3.

11. P. Serrano, M. A. Johnson, A. Chatterjee, B. Pedrini, and K. Wuthrich.. Biomol NMR Assign. 2008, 2, 135–138. NMR assignment of the nonstructural protein nsp3(1066–1181) from SARS-CoV.

12. Chatterjee, A., Johnson, M.A., Serrano, P., Pedrini, B. and Wüthrich, K. 2007 Biomol. NMR Assign. 1, 191–194. NMR assignment of the domain 513–651 from the SARS-CoV nonstructural protein nsp3.

13. P. Serrano , M. A. Johnson, M. S. Almeida, R. Horst, T. Herrmann, J. S. Joseph, B. W. Neuman, V. Subramanian, K. S. Saikatendu, M. J. Buchmeier, R. C. Stevens, P. Kuhn, K. Wüthrich. J. Virol. 2007, 12049–12060. NMR Structure of the N-terminal Domain of the Nonstructural Protein 3 from the SARS Coronavirus.

14. P. Serrano, M. Ejido-Gabas, A. Llebaria, A. Delgado. Tetrahedrom Asymethy. 2007. 1971–1974 . An unexpected access to 5-epi-cyclophellitol, a new cyclitol member.

15. P. Serrano, J. Casas, A. Llebaria, M. Zucco, G. Emeric, A. Delgado. J. Comb. Chem. 2007, 9, 635-643. Parallel Synthesis and yeast growth inhibition screening of succinamic acid libraries.

16. P. Serrano, J.Casas , A. Llebaria, M. Zucco, G. Emeric, A. Delgado. J. Comb. Chem. 2007, 9, 43-52. Combinatorial approach to N-Substituted Aminocyclitol Libraries by Solution-Phase Parallel synthesis and Preliminary Evaluation as Glucocerebroside inhibitors.

17. P. Serrano, M.S. Almeida, M. A. Johnson, K. Wuthrich,. J. Biomol. NMR. 2006, 36, 45. NMR assignment of the protein nsp3a from SARS coronavirus

18. P. Serrano, A. Llebaria, J. Vazquez, J.M. Anglada, A. Delgado. Chem. Eur. J. 2005, 11, 4465-4472. On the regio- and stereoselective synthesis of aminocyclitols from cyclitol epoxides. The effect of Li as a Chelating agent.

19. P. Serrano, A. Llebaria, A. Delgado. Regio- and stereoselective synthesis of aminoinositols and 1,2-diaminoinositols from conduritol B epoxide. J. Org. Chem. 2005, 70, 7829-7840.

20. M. Ejido-Gabas, P. Serrano, Casas, J. Llebaria, A., Delgado, A. New aminocyclitols as modulators of glucosylceramide metabolism. Org. Biomol. Chem. 2005, 7, 1195–1201.

21. P. Serrano, A. Llebaria, A. Delgado. An unexpected chelation controlled by Yb(OTf)3 catalyzed aminolysis and azidolysis of cyclitol epoxides. J. Org. Chem. 2002, 67, 7165–7167.