Guillermo Calero
This email address is being protected from spambots. You need JavaScript enabled to view it. 
Phone (412) 383-5319
Fax (412) 648-9008

University of Pittsburgh
1040 Biomedical Science Tower 3

 

Guillermo Calero


Associate Professor
Department of Structural Biology



My laboratory at the University of Pittsburgh, works on reconstitution of multi-protein complexes (MPCs) for biochemical and X-ray crystallographic studies. In particular we are interested in MPCs involved in: 1) nuclear events such as transcription initiation and DNA repair, and 2) Interactions of membrane receptors with their cytoplasmic partners. Since MPCs cannot be isolated as a whole from cells, we have developed biochemical tools that have allowed us to express and purify individual components (monomeric or multimeric) to reconstitute such MPCs. Our ultimate goals is to crystallize and perform structural studies using X-ray crystallography of these samples which posses great biological interest. We are also participating in development of methods using EM to identify best diffracting nano-crystals for femtosecond diffraction experiments.

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Education & Training

Graduate
Baylor College of Medicine
Facultad de Medicina, UNAM
M.D. 1991

Cornell University
Ph.D. 2003 in Chemistry and Chemical Biology

Postgraduate
Stanford University
Postdoctoral Scholar 2003-2008



Representative Publications


Murakami K, Calero G, Brown CR, Liu X, Davis RE, Boeger H and Kornberg RD (2013). Formation and fate of a complete, 31-Protein, RNA polymerase II transcription initiaition complex. Journal of Biological Chemistry.

Wehbi VL, Stevenson HP, Feinstein TN, Calero G, Romero, G and Vilardaga JP (2013). Non-canonical GPCR signaling arising from  a PTH-arrestin-GS complex. Proc Natl Acad Sci U S A. 110(4):1530-5.

Stevenson HP, Mahkov AM, Calero M, Mathews I, Lin G, Santamaria H, Ross TM, Soltis M, Koshla S, Conway J, Cohen A and Calero G (2014).  Electron Microscopy Screening   of Protein Nano crystals for Serial Femtosecond Crystallography. Proc Natl Acad Sci U S A. 111(23):8470-5.

Stevenson H.P., DePonte D.P., Makhov A.M., Zeldin O.B., Calero G*, and Cohen A.E* (2014). Transmission electron microscopy as a tool for nano-crystal characterization pre- and post-injector. Philosophical Transations B. Philosophical Transactions B. 17;369:1647 * Corresponding author

Calero G, Cohen A.E, Luft J.R and Snell E (2014). Identifying, studying and making good use of macromolecular crystals. Acta Crystallographica F. 70:993-1008


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Active Grants


Structural Studies of RNA Polymerase II Transcription Initiation and Elongation
01/15/15 – 12/31/19
National Institutes of Health
R01

Structural and Functional Mechanisms of PTH-Receptor Signaling
07/01/14 – 05/31/18
National Institutes of Health
R01

 


 

Angela Gronenborn

Jinwoo Ahn

James Conway

Rieko Ishima

   

Yan Xu

Peijun Zhang

Ronald Wetzel

Patrick van der Wel

   

 

 

         
           
           
           

Angela M Gronenborn
This email address is being protected from spambots. You need JavaScript enabled to view it. 
Phone (412) 648-9959
Fax (412) 648-9008

University of Pittsburgh
1050 Biomedical Science Tower 3

 

Angela Gronenborn

UPMC Rosalind Franklin Professor and Chair
Department of Structural Biology
Distinguished Professor of Structural Biology
University of Pittsburgh School of Medicine
Professor of Bioengineering
Swanson School of Engineering


In order to understand how biological macromolecules work and to intervene with respect to activity and function, detailed knowledge of their architecture and dynamic features is required. Characterizing the major determinants for stability and conformational specificity of normal and disease-causing forms of important molecules allows one to unravel the complex processes associated with disease. Angela Gronenborn's research combines nuclear magnetic resonance (NMR) spectroscopy and other structural techniques with biophysics, biochemistry, and chemistry in an integrative fashion to investigate cellular processes at the molecular and atomic levels in relation to human disease. Within her group, NMR methods for determining three-dimensional structures of biological macromolecules are developed and applied to challenging systems. As such, the Gronenborn group has solved structures of a large number of medically and biologically important proteins and protein complexes, such as various HIV and AIDS related proteins.  

Visit Angela's lab website


Education & Training

Undergraduate
University of Cologne, Cologne, Germany
Vordiplom, 1972 in Chemistry, Physics

Postgraduate
University of Cologne, Cologne, Germany
Diplom (MS), 1975 in Chemistry

University of Cologne, Cologne, Germany
Dr.rer.nat. (PhD), 1978, summa cum laude, in Organic Chemistry

National Institute for Medical Research, Mill Hill, London
Division of Molecular Pharmacology, Advisor:  James Feeney


Selected Awards and Honors


2007 Elected to Membership in the National Academy of Sciences
2010 Elected to the Norwegian Academy of Science and Letters
2014 Life Science Award, Carnegie Science Awards
2014 Elected to the Germany Academy of Sciences
2018 Elected to the American Academy of Arts and Sciences
2018 ASBMB Mildred Cohn Award in Biological Chemistry
2019 Richard R. Ernst Prize in Magnetic Resonance
2020 E. Bright Wilson Award in Spectroscopy



Representative Publications


Gronenborn AM, Birdsall B, Hyde EI, Roberts GCK, Feeney J, Burgen ASV.  Direct observation by NMR of two coexisting conformations of an enzyme-ligand complex in solution.  Nature 230, 273 (1980).

 

Oschkinat H, Griesinger C, Kraulis PJ, Sørensen OW, Ernst RR, Gronenborn AM, Clore GM. Three-dimensional NMR spectroscopy of a protein in solution. Nature 332, 374 (1988).

 

Clore GM, Gronenborn AM.  Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy. Science 252, 1390 (1991).

 

Omichinski JG, Clore GM, Schaad O, Felsenfeld G, Traino, C, Appella E, Stahl SJ, Gronenborn AM.   NMR structure of a specific DNA complex of Zn-containing DNA binding domain of GATA-1. Science 261, 438-446 (1993).

 

Frank MK, Dyda F, Dobrodumov A, Gronenborn AM.  Core mutations switch monomeric protein GB1 into an intertwined tetramer.  Nat. Struct. Biol., 9(11): 877-885 (2002).

 

Byeon, IL, Meng X, Jung J, Zhao G, Yang R, Ahn J, Shi J, Concel J, Aiken C, Zhang P, Gronenborn AM. Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function. Cell 139, 780 (2009). PMC2782912

 

Ahn J, Vu T, Novince Z, Guerrero-Santoro J, Rapic-Otrin V, Gronenborn AM. HIV-1 Vpr loads Uracil DNA Glycosylase-2 onto DCAF1, a substrate recognition subunit of a Cullin 4A-RING E3 ubiquitin ligase for proteasome-dependent degradation. J Biol Chem 285, 37333 (2010). PMC2988339

 

Byeon I-JL, Ahn J, Mitra, M, Byeon C-H, Hercik, K, Hritz J, Charlton LM, Levin JG, Gronenborn AM.  NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity.  Nature Comm 4 1890 (2013). PMC3674325

 

Zhao G, Perilla JR, Yufenyuy EL, Meng X, Chen B, Ning J, Ahn J, Gronenborn AM, Schulten K, Aiken C, Zhang P. Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics.  Nature 497, 643 (2013). PMC3729984

 

Boatz JC, Whitley MJ, Li M, Gronenborn AM, van der Wel PCA. Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.   Nat Commun. 8:15137 (2017).  PMC5424181 

 

Wang M, Quinn CM, Perilla JR, Zhang H, Shirra R Jr, Hou G, Byeon IJ, Suiter CL, Ablan S, Urano E, Nitz TJ, Aiken C, Freed EO, Zhang P, Schulten K, Gronenborn AM, Polenova T. Quenching protein dynamics interferes with HIV capsid maturation.  Nat Commun. 8:1779 (2017).  PMC5701193
 

Lu M, Sarkar S, Wang M, Kraus J, Fritz M, Quinn CM, Bai S, Holmes ST, Dybowski C, Yap GPA, Struppe J, Sergeyev IV, Maas W, Gronenborn AM, Polenova T. 19F Magic Angle Spinning NMR Spectroscopy and Density Functional Theory Calculations of Fluorosubstituted Tryptophans: Integrating Experiment and Theory for Accurate Determination of Chemical Shift Tensors.  J Phys Chem B.122:6148 (2018).  

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Active Grants


Structural Characterization of Interacting and Aggregating Cataract-associated Crystallins
09/30/19 to 07/31/23
National Institutes of Health
R01

 

University of Pittsburgh Center for HIV Protein Interactions (PCHPI)

08/27/2007 to 7/31/22

National Institutes of Health

P50

 

Allosteric regulation of SIRT1 by a PACS-2 and DBC1 regulatory hub

08/23/2017 to 6/30/21

National Institutes of Health

R01

 

Development of Fluorine Nuclear Magnetic Resonance (NMR) Spectroscopy as a Versatile Probe of Structure and Chemical Environment in Proteins

08/01/2017 to 7/31/21
National Science Foundation